Source 1primary paper1994PLANT PHYSIOLOGY
Toolkit/native green gel system
native green gel system
Taxonomy: Technique Branch / Method. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
The native green gel system is an assay method used to study light-induced assembly of chlorophyll-protein complexes during greening. In etiolated barley (Hordeum vulgare), it was used to resolve LHCII-associated bands and follow the appearance of type 1, type 2, and type 3 LHCII apoproteins during illumination.
Usefulness & Problems
Why this is useful
This method is useful for monitoring how chlorophyll-protein complexes assemble in response to light during seedling greening. In the cited barley study, it enabled analysis of LHCII apoprotein accumulation kinetics and assessment of whether higher molecular mass forms of type 1 and type 3 LHCII apoproteins were detectable.
Problem solved
It addresses the problem of tracking light-dependent formation of photosynthetic pigment-protein complexes in developing plastids. Specifically, it provided a way to examine the appearance of type 1, type 2, and type 3 LHCII apoproteins during greening of etiolated barley seedlings.
Problem links
Need precise spatiotemporal control with light input
DerivedThe native green gel system is an assay method used to study light-induced assembly of chlorophyll-protein complexes during greening. In etiolated barley (Hordeum vulgare), it was used to resolve LHCII-associated bands and follow the appearance of type 1, type 2, and type 3 LHCII apoproteins during illumination.
Taxonomy & Function
Primary hierarchy
Technique Branch
Method: A concrete measurement method used to characterize an engineered system.
Mechanisms
immunoblot-based band identificationlight-dependent assembly readoutnative electrophoretic separationTechniques
Functional AssayTarget processes
No target processes tagged yet.
Input: Light
Implementation Constraints
cofactor dependency: cofactor requirement unknownencoding mode: genetically encodedimplementation constraint: context specific validationimplementation constraint: spectral hardware requirementoperating role: sensor
The assay was used to study greening under light input in etiolated barley seedlings and was paired with identification of LHCII apoprotein bands by immunoblotting. The supplied evidence does not specify construct requirements, cofactors, instrumentation settings, or detailed electrophoresis conditions.
The evidence is limited to a single cited study in etiolated barley and does not establish performance across organisms, tissues, or other chlorophyll-protein complexes. Available evidence does not provide technical parameters such as gel composition, sensitivity, quantitative range, or reproducibility metrics.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
No corresponding higher molecular mass forms of type 1 and type 3 LHCII apoproteins were detected.
No corresponding higher molecular mass forms of type 1 and 3 LHCII apoproteins could be detected
No corresponding higher molecular mass forms of type 1 and type 3 LHCII apoproteins were detected.
No corresponding higher molecular mass forms of type 1 and 3 LHCII apoproteins could be detected
No corresponding higher molecular mass forms of type 1 and type 3 LHCII apoproteins were detected.
No corresponding higher molecular mass forms of type 1 and 3 LHCII apoproteins could be detected
No corresponding higher molecular mass forms of type 1 and type 3 LHCII apoproteins were detected.
No corresponding higher molecular mass forms of type 1 and 3 LHCII apoproteins could be detected
No corresponding higher molecular mass forms of type 1 and type 3 LHCII apoproteins were detected.
No corresponding higher molecular mass forms of type 1 and 3 LHCII apoproteins could be detected
No corresponding higher molecular mass forms of type 1 and type 3 LHCII apoproteins were detected.
No corresponding higher molecular mass forms of type 1 and 3 LHCII apoproteins could be detected
No corresponding higher molecular mass forms of type 1 and type 3 LHCII apoproteins were detected.
No corresponding higher molecular mass forms of type 1 and 3 LHCII apoproteins could be detected
No corresponding higher molecular mass forms of type 1 and type 3 LHCII apoproteins were detected.
No corresponding higher molecular mass forms of type 1 and 3 LHCII apoproteins could be detected
No corresponding higher molecular mass forms of type 1 and type 3 LHCII apoproteins were detected.
No corresponding higher molecular mass forms of type 1 and 3 LHCII apoproteins could be detected
No corresponding higher molecular mass forms of type 1 and type 3 LHCII apoproteins were detected.
No corresponding higher molecular mass forms of type 1 and 3 LHCII apoproteins could be detected
No corresponding higher molecular mass forms of type 1 and type 3 LHCII apoproteins were detected.
No corresponding higher molecular mass forms of type 1 and 3 LHCII apoproteins could be detected
No corresponding higher molecular mass forms of type 1 and type 3 LHCII apoproteins were detected.
No corresponding higher molecular mass forms of type 1 and 3 LHCII apoproteins could be detected
No corresponding higher molecular mass forms of type 1 and type 3 LHCII apoproteins were detected.
No corresponding higher molecular mass forms of type 1 and 3 LHCII apoproteins could be detected
No corresponding higher molecular mass forms of type 1 and type 3 LHCII apoproteins were detected.
No corresponding higher molecular mass forms of type 1 and 3 LHCII apoproteins could be detected
During light-induced greening of etiolated barley seedlings, type 1, type 2, and type 3 LHCII apoproteins accumulate simultaneously and at similar rates.
During light-induced greening of 6-d-old etiolated barley seedlings, the type 1, 2, and 3 LHCII apoproteins accumulate simultaneously and at similar rates
During light-induced greening of etiolated barley seedlings, type 1, type 2, and type 3 LHCII apoproteins accumulate simultaneously and at similar rates.
During light-induced greening of 6-d-old etiolated barley seedlings, the type 1, 2, and 3 LHCII apoproteins accumulate simultaneously and at similar rates
During light-induced greening of etiolated barley seedlings, type 1, type 2, and type 3 LHCII apoproteins accumulate simultaneously and at similar rates.
During light-induced greening of 6-d-old etiolated barley seedlings, the type 1, 2, and 3 LHCII apoproteins accumulate simultaneously and at similar rates
During light-induced greening of etiolated barley seedlings, type 1, type 2, and type 3 LHCII apoproteins accumulate simultaneously and at similar rates.
During light-induced greening of 6-d-old etiolated barley seedlings, the type 1, 2, and 3 LHCII apoproteins accumulate simultaneously and at similar rates
During light-induced greening of etiolated barley seedlings, type 1, type 2, and type 3 LHCII apoproteins accumulate simultaneously and at similar rates.
During light-induced greening of 6-d-old etiolated barley seedlings, the type 1, 2, and 3 LHCII apoproteins accumulate simultaneously and at similar rates
During light-induced greening of etiolated barley seedlings, type 1, type 2, and type 3 LHCII apoproteins accumulate simultaneously and at similar rates.
During light-induced greening of 6-d-old etiolated barley seedlings, the type 1, 2, and 3 LHCII apoproteins accumulate simultaneously and at similar rates
During light-induced greening of etiolated barley seedlings, type 1, type 2, and type 3 LHCII apoproteins accumulate simultaneously and at similar rates.
During light-induced greening of 6-d-old etiolated barley seedlings, the type 1, 2, and 3 LHCII apoproteins accumulate simultaneously and at similar rates
During light-induced greening of etiolated barley seedlings, type 1, type 2, and type 3 LHCII apoproteins accumulate simultaneously and at similar rates.
During light-induced greening of 6-d-old etiolated barley seedlings, the type 1, 2, and 3 LHCII apoproteins accumulate simultaneously and at similar rates
During light-induced greening of etiolated barley seedlings, type 1, type 2, and type 3 LHCII apoproteins accumulate simultaneously and at similar rates.
During light-induced greening of 6-d-old etiolated barley seedlings, the type 1, 2, and 3 LHCII apoproteins accumulate simultaneously and at similar rates
During light-induced greening of etiolated barley seedlings, type 1, type 2, and type 3 LHCII apoproteins accumulate simultaneously and at similar rates.
During light-induced greening of 6-d-old etiolated barley seedlings, the type 1, 2, and 3 LHCII apoproteins accumulate simultaneously and at similar rates
During light-induced greening of etiolated barley seedlings, type 1, type 2, and type 3 LHCII apoproteins accumulate simultaneously and at similar rates.
During light-induced greening of 6-d-old etiolated barley seedlings, the type 1, 2, and 3 LHCII apoproteins accumulate simultaneously and at similar rates
During light-induced greening of etiolated barley seedlings, type 1, type 2, and type 3 LHCII apoproteins accumulate simultaneously and at similar rates.
During light-induced greening of 6-d-old etiolated barley seedlings, the type 1, 2, and 3 LHCII apoproteins accumulate simultaneously and at similar rates
During light-induced greening of etiolated barley seedlings, type 1, type 2, and type 3 LHCII apoproteins accumulate simultaneously and at similar rates.
During light-induced greening of 6-d-old etiolated barley seedlings, the type 1, 2, and 3 LHCII apoproteins accumulate simultaneously and at similar rates
During light-induced greening of etiolated barley seedlings, type 1, type 2, and type 3 LHCII apoproteins accumulate simultaneously and at similar rates.
During light-induced greening of 6-d-old etiolated barley seedlings, the type 1, 2, and 3 LHCII apoproteins accumulate simultaneously and at similar rates
Western blot analysis identified the 26.0 kD lowest LHCII band as containing type 3 LHCII apoproteins.
the lowest band at 26.0 kD as containing the type 3 LHCII apoproteins
molecular mass 26 kD
Western blot analysis identified the 26.0 kD lowest LHCII band as containing type 3 LHCII apoproteins.
the lowest band at 26.0 kD as containing the type 3 LHCII apoproteins
molecular mass 26 kD
Western blot analysis identified the 26.0 kD lowest LHCII band as containing type 3 LHCII apoproteins.
the lowest band at 26.0 kD as containing the type 3 LHCII apoproteins
molecular mass 26 kD
Western blot analysis identified the 26.0 kD lowest LHCII band as containing type 3 LHCII apoproteins.
the lowest band at 26.0 kD as containing the type 3 LHCII apoproteins
molecular mass 26 kD
Western blot analysis identified the 26.0 kD lowest LHCII band as containing type 3 LHCII apoproteins.
the lowest band at 26.0 kD as containing the type 3 LHCII apoproteins
molecular mass 26 kD
Western blot analysis identified the 26.0 kD lowest LHCII band as containing type 3 LHCII apoproteins.
the lowest band at 26.0 kD as containing the type 3 LHCII apoproteins
molecular mass 26 kD
Western blot analysis identified the 26.0 kD lowest LHCII band as containing type 3 LHCII apoproteins.
the lowest band at 26.0 kD as containing the type 3 LHCII apoproteins
molecular mass 26 kD
Western blot analysis identified the 26.0 kD lowest LHCII band as containing type 3 LHCII apoproteins.
the lowest band at 26.0 kD as containing the type 3 LHCII apoproteins
molecular mass 26 kD
Western blot analysis identified the 26.0 kD lowest LHCII band as containing type 3 LHCII apoproteins.
the lowest band at 26.0 kD as containing the type 3 LHCII apoproteins
molecular mass 26 kD
Western blot analysis identified the 26.0 kD lowest LHCII band as containing type 3 LHCII apoproteins.
the lowest band at 26.0 kD as containing the type 3 LHCII apoproteins
molecular mass 26 kD
Western blot analysis identified the 26.0 kD lowest LHCII band as containing type 3 LHCII apoproteins.
the lowest band at 26.0 kD as containing the type 3 LHCII apoproteins
molecular mass 26 kD
Western blot analysis identified the 26.0 kD lowest LHCII band as containing type 3 LHCII apoproteins.
the lowest band at 26.0 kD as containing the type 3 LHCII apoproteins
molecular mass 26 kD
Western blot analysis identified the 26.0 kD lowest LHCII band as containing type 3 LHCII apoproteins.
the lowest band at 26.0 kD as containing the type 3 LHCII apoproteins
molecular mass 26 kD
Western blot analysis identified the 26.0 kD lowest LHCII band as containing type 3 LHCII apoproteins.
the lowest band at 26.0 kD as containing the type 3 LHCII apoproteins
molecular mass 26 kD
Western blot analysis identified the 26.9 kD middle LHCII band as containing type 1 LHCII apoproteins.
the middle band at 26.9 kD as containing the type 1 LHCII apoproteins
molecular mass 26.9 kD
Western blot analysis identified the 26.9 kD middle LHCII band as containing type 1 LHCII apoproteins.
the middle band at 26.9 kD as containing the type 1 LHCII apoproteins
molecular mass 26.9 kD
Western blot analysis identified the 26.9 kD middle LHCII band as containing type 1 LHCII apoproteins.
the middle band at 26.9 kD as containing the type 1 LHCII apoproteins
molecular mass 26.9 kD
Western blot analysis identified the 26.9 kD middle LHCII band as containing type 1 LHCII apoproteins.
the middle band at 26.9 kD as containing the type 1 LHCII apoproteins
molecular mass 26.9 kD
Western blot analysis identified the 26.9 kD middle LHCII band as containing type 1 LHCII apoproteins.
the middle band at 26.9 kD as containing the type 1 LHCII apoproteins
molecular mass 26.9 kD
Western blot analysis identified the 26.9 kD middle LHCII band as containing type 1 LHCII apoproteins.
the middle band at 26.9 kD as containing the type 1 LHCII apoproteins
molecular mass 26.9 kD
Western blot analysis identified the 26.9 kD middle LHCII band as containing type 1 LHCII apoproteins.
the middle band at 26.9 kD as containing the type 1 LHCII apoproteins
molecular mass 26.9 kD
Western blot analysis identified the 26.9 kD middle LHCII band as containing type 1 LHCII apoproteins.
the middle band at 26.9 kD as containing the type 1 LHCII apoproteins
molecular mass 26.9 kD
Western blot analysis identified the 26.9 kD middle LHCII band as containing type 1 LHCII apoproteins.
the middle band at 26.9 kD as containing the type 1 LHCII apoproteins
molecular mass 26.9 kD
Western blot analysis identified the 26.9 kD middle LHCII band as containing type 1 LHCII apoproteins.
the middle band at 26.9 kD as containing the type 1 LHCII apoproteins
molecular mass 26.9 kD
Western blot analysis identified the 26.9 kD middle LHCII band as containing type 1 LHCII apoproteins.
the middle band at 26.9 kD as containing the type 1 LHCII apoproteins
molecular mass 26.9 kD
Western blot analysis identified the 26.9 kD middle LHCII band as containing type 1 LHCII apoproteins.
the middle band at 26.9 kD as containing the type 1 LHCII apoproteins
molecular mass 26.9 kD
Western blot analysis identified the 26.9 kD middle LHCII band as containing type 1 LHCII apoproteins.
the middle band at 26.9 kD as containing the type 1 LHCII apoproteins
molecular mass 26.9 kD
Western blot analysis identified the 26.9 kD middle LHCII band as containing type 1 LHCII apoproteins.
the middle band at 26.9 kD as containing the type 1 LHCII apoproteins
molecular mass 26.9 kD
Western blot analysis identified the 27.5 kD highest molecular mass LHCII band as containing type 2 LHCII apoproteins.
Western blot analysis of the three major LHCII apoprotein bands has identified the highest molecular mass band at 27.5 kD as containing the type 2 LHCII apoproteins
molecular mass 27.5 kD
Western blot analysis identified the 27.5 kD highest molecular mass LHCII band as containing type 2 LHCII apoproteins.
Western blot analysis of the three major LHCII apoprotein bands has identified the highest molecular mass band at 27.5 kD as containing the type 2 LHCII apoproteins
molecular mass 27.5 kD
Western blot analysis identified the 27.5 kD highest molecular mass LHCII band as containing type 2 LHCII apoproteins.
Western blot analysis of the three major LHCII apoprotein bands has identified the highest molecular mass band at 27.5 kD as containing the type 2 LHCII apoproteins
molecular mass 27.5 kD
Western blot analysis identified the 27.5 kD highest molecular mass LHCII band as containing type 2 LHCII apoproteins.
Western blot analysis of the three major LHCII apoprotein bands has identified the highest molecular mass band at 27.5 kD as containing the type 2 LHCII apoproteins
molecular mass 27.5 kD
Western blot analysis identified the 27.5 kD highest molecular mass LHCII band as containing type 2 LHCII apoproteins.
Western blot analysis of the three major LHCII apoprotein bands has identified the highest molecular mass band at 27.5 kD as containing the type 2 LHCII apoproteins
molecular mass 27.5 kD
Western blot analysis identified the 27.5 kD highest molecular mass LHCII band as containing type 2 LHCII apoproteins.
Western blot analysis of the three major LHCII apoprotein bands has identified the highest molecular mass band at 27.5 kD as containing the type 2 LHCII apoproteins
molecular mass 27.5 kD
Western blot analysis identified the 27.5 kD highest molecular mass LHCII band as containing type 2 LHCII apoproteins.
Western blot analysis of the three major LHCII apoprotein bands has identified the highest molecular mass band at 27.5 kD as containing the type 2 LHCII apoproteins
molecular mass 27.5 kD
Western blot analysis identified the 27.5 kD highest molecular mass LHCII band as containing type 2 LHCII apoproteins.
Western blot analysis of the three major LHCII apoprotein bands has identified the highest molecular mass band at 27.5 kD as containing the type 2 LHCII apoproteins
molecular mass 27.5 kD
Western blot analysis identified the 27.5 kD highest molecular mass LHCII band as containing type 2 LHCII apoproteins.
Western blot analysis of the three major LHCII apoprotein bands has identified the highest molecular mass band at 27.5 kD as containing the type 2 LHCII apoproteins
molecular mass 27.5 kD
Western blot analysis identified the 27.5 kD highest molecular mass LHCII band as containing type 2 LHCII apoproteins.
Western blot analysis of the three major LHCII apoprotein bands has identified the highest molecular mass band at 27.5 kD as containing the type 2 LHCII apoproteins
molecular mass 27.5 kD
Western blot analysis identified the 27.5 kD highest molecular mass LHCII band as containing type 2 LHCII apoproteins.
Western blot analysis of the three major LHCII apoprotein bands has identified the highest molecular mass band at 27.5 kD as containing the type 2 LHCII apoproteins
molecular mass 27.5 kD
Western blot analysis identified the 27.5 kD highest molecular mass LHCII band as containing type 2 LHCII apoproteins.
Western blot analysis of the three major LHCII apoprotein bands has identified the highest molecular mass band at 27.5 kD as containing the type 2 LHCII apoproteins
molecular mass 27.5 kD
Western blot analysis identified the 27.5 kD highest molecular mass LHCII band as containing type 2 LHCII apoproteins.
Western blot analysis of the three major LHCII apoprotein bands has identified the highest molecular mass band at 27.5 kD as containing the type 2 LHCII apoproteins
molecular mass 27.5 kD
Western blot analysis identified the 27.5 kD highest molecular mass LHCII band as containing type 2 LHCII apoproteins.
Western blot analysis of the three major LHCII apoprotein bands has identified the highest molecular mass band at 27.5 kD as containing the type 2 LHCII apoproteins
molecular mass 27.5 kD
Differences remain apparent in chlorophyll-protein complex composition between light-control plants and etiolated plants greened for 8 days.
differences are still apparent in the composition of chlorophyll-protein complexes of light-control plants and those of etiolated plants greened for 8 d
greening duration 8 d
Differences remain apparent in chlorophyll-protein complex composition between light-control plants and etiolated plants greened for 8 days.
differences are still apparent in the composition of chlorophyll-protein complexes of light-control plants and those of etiolated plants greened for 8 d
greening duration 8 d
Differences remain apparent in chlorophyll-protein complex composition between light-control plants and etiolated plants greened for 8 days.
differences are still apparent in the composition of chlorophyll-protein complexes of light-control plants and those of etiolated plants greened for 8 d
greening duration 8 d
Differences remain apparent in chlorophyll-protein complex composition between light-control plants and etiolated plants greened for 8 days.
differences are still apparent in the composition of chlorophyll-protein complexes of light-control plants and those of etiolated plants greened for 8 d
greening duration 8 d
Differences remain apparent in chlorophyll-protein complex composition between light-control plants and etiolated plants greened for 8 days.
differences are still apparent in the composition of chlorophyll-protein complexes of light-control plants and those of etiolated plants greened for 8 d
greening duration 8 d
Differences remain apparent in chlorophyll-protein complex composition between light-control plants and etiolated plants greened for 8 days.
differences are still apparent in the composition of chlorophyll-protein complexes of light-control plants and those of etiolated plants greened for 8 d
greening duration 8 d
Differences remain apparent in chlorophyll-protein complex composition between light-control plants and etiolated plants greened for 8 days.
differences are still apparent in the composition of chlorophyll-protein complexes of light-control plants and those of etiolated plants greened for 8 d
greening duration 8 d
Differences remain apparent in chlorophyll-protein complex composition between light-control plants and etiolated plants greened for 8 days.
differences are still apparent in the composition of chlorophyll-protein complexes of light-control plants and those of etiolated plants greened for 8 d
greening duration 8 d
Differences remain apparent in chlorophyll-protein complex composition between light-control plants and etiolated plants greened for 8 days.
differences are still apparent in the composition of chlorophyll-protein complexes of light-control plants and those of etiolated plants greened for 8 d
greening duration 8 d
Differences remain apparent in chlorophyll-protein complex composition between light-control plants and etiolated plants greened for 8 days.
differences are still apparent in the composition of chlorophyll-protein complexes of light-control plants and those of etiolated plants greened for 8 d
greening duration 8 d
Differences remain apparent in chlorophyll-protein complex composition between light-control plants and etiolated plants greened for 8 days.
differences are still apparent in the composition of chlorophyll-protein complexes of light-control plants and those of etiolated plants greened for 8 d
greening duration 8 d
Differences remain apparent in chlorophyll-protein complex composition between light-control plants and etiolated plants greened for 8 days.
differences are still apparent in the composition of chlorophyll-protein complexes of light-control plants and those of etiolated plants greened for 8 d
greening duration 8 d
Differences remain apparent in chlorophyll-protein complex composition between light-control plants and etiolated plants greened for 8 days.
differences are still apparent in the composition of chlorophyll-protein complexes of light-control plants and those of etiolated plants greened for 8 d
greening duration 8 d
Differences remain apparent in chlorophyll-protein complex composition between light-control plants and etiolated plants greened for 8 days.
differences are still apparent in the composition of chlorophyll-protein complexes of light-control plants and those of etiolated plants greened for 8 d
greening duration 8 d
During the 8-24 h rapid phase of thylakoid development, two slightly larger type 2 LHCII apoproteins of 28.3 and 28.7 kD also accumulate in thylakoids.
During the most rapid phase of thylakoid development (8-24 h), two slightly larger (28.3 and 28.7 kD) type 2 LHCII apoproteins (precursor intermediates?) also accumulate in the thylakoids
molecular mass 28.3 kDmolecular mass 28.7 kDtime window 8-24 h
During the 8-24 h rapid phase of thylakoid development, two slightly larger type 2 LHCII apoproteins of 28.3 and 28.7 kD also accumulate in thylakoids.
During the most rapid phase of thylakoid development (8-24 h), two slightly larger (28.3 and 28.7 kD) type 2 LHCII apoproteins (precursor intermediates?) also accumulate in the thylakoids
molecular mass 28.3 kDmolecular mass 28.7 kDtime window 8-24 h
During the 8-24 h rapid phase of thylakoid development, two slightly larger type 2 LHCII apoproteins of 28.3 and 28.7 kD also accumulate in thylakoids.
During the most rapid phase of thylakoid development (8-24 h), two slightly larger (28.3 and 28.7 kD) type 2 LHCII apoproteins (precursor intermediates?) also accumulate in the thylakoids
molecular mass 28.3 kDmolecular mass 28.7 kDtime window 8-24 h
During the 8-24 h rapid phase of thylakoid development, two slightly larger type 2 LHCII apoproteins of 28.3 and 28.7 kD also accumulate in thylakoids.
During the most rapid phase of thylakoid development (8-24 h), two slightly larger (28.3 and 28.7 kD) type 2 LHCII apoproteins (precursor intermediates?) also accumulate in the thylakoids
molecular mass 28.3 kDmolecular mass 28.7 kDtime window 8-24 h
During the 8-24 h rapid phase of thylakoid development, two slightly larger type 2 LHCII apoproteins of 28.3 and 28.7 kD also accumulate in thylakoids.
During the most rapid phase of thylakoid development (8-24 h), two slightly larger (28.3 and 28.7 kD) type 2 LHCII apoproteins (precursor intermediates?) also accumulate in the thylakoids
molecular mass 28.3 kDmolecular mass 28.7 kDtime window 8-24 h
During the 8-24 h rapid phase of thylakoid development, two slightly larger type 2 LHCII apoproteins of 28.3 and 28.7 kD also accumulate in thylakoids.
During the most rapid phase of thylakoid development (8-24 h), two slightly larger (28.3 and 28.7 kD) type 2 LHCII apoproteins (precursor intermediates?) also accumulate in the thylakoids
molecular mass 28.3 kDmolecular mass 28.7 kDtime window 8-24 h
During the 8-24 h rapid phase of thylakoid development, two slightly larger type 2 LHCII apoproteins of 28.3 and 28.7 kD also accumulate in thylakoids.
During the most rapid phase of thylakoid development (8-24 h), two slightly larger (28.3 and 28.7 kD) type 2 LHCII apoproteins (precursor intermediates?) also accumulate in the thylakoids
molecular mass 28.3 kDmolecular mass 28.7 kDtime window 8-24 h
During the 8-24 h rapid phase of thylakoid development, two slightly larger type 2 LHCII apoproteins of 28.3 and 28.7 kD also accumulate in thylakoids.
During the most rapid phase of thylakoid development (8-24 h), two slightly larger (28.3 and 28.7 kD) type 2 LHCII apoproteins (precursor intermediates?) also accumulate in the thylakoids
molecular mass 28.3 kDmolecular mass 28.7 kDtime window 8-24 h
During the 8-24 h rapid phase of thylakoid development, two slightly larger type 2 LHCII apoproteins of 28.3 and 28.7 kD also accumulate in thylakoids.
During the most rapid phase of thylakoid development (8-24 h), two slightly larger (28.3 and 28.7 kD) type 2 LHCII apoproteins (precursor intermediates?) also accumulate in the thylakoids
molecular mass 28.3 kDmolecular mass 28.7 kDtime window 8-24 h
During the 8-24 h rapid phase of thylakoid development, two slightly larger type 2 LHCII apoproteins of 28.3 and 28.7 kD also accumulate in thylakoids.
During the most rapid phase of thylakoid development (8-24 h), two slightly larger (28.3 and 28.7 kD) type 2 LHCII apoproteins (precursor intermediates?) also accumulate in the thylakoids
molecular mass 28.3 kDmolecular mass 28.7 kDtime window 8-24 h
During the 8-24 h rapid phase of thylakoid development, two slightly larger type 2 LHCII apoproteins of 28.3 and 28.7 kD also accumulate in thylakoids.
During the most rapid phase of thylakoid development (8-24 h), two slightly larger (28.3 and 28.7 kD) type 2 LHCII apoproteins (precursor intermediates?) also accumulate in the thylakoids
molecular mass 28.3 kDmolecular mass 28.7 kDtime window 8-24 h
During the 8-24 h rapid phase of thylakoid development, two slightly larger type 2 LHCII apoproteins of 28.3 and 28.7 kD also accumulate in thylakoids.
During the most rapid phase of thylakoid development (8-24 h), two slightly larger (28.3 and 28.7 kD) type 2 LHCII apoproteins (precursor intermediates?) also accumulate in the thylakoids
molecular mass 28.3 kDmolecular mass 28.7 kDtime window 8-24 h
During the 8-24 h rapid phase of thylakoid development, two slightly larger type 2 LHCII apoproteins of 28.3 and 28.7 kD also accumulate in thylakoids.
During the most rapid phase of thylakoid development (8-24 h), two slightly larger (28.3 and 28.7 kD) type 2 LHCII apoproteins (precursor intermediates?) also accumulate in the thylakoids
molecular mass 28.3 kDmolecular mass 28.7 kDtime window 8-24 h
During the 8-24 h rapid phase of thylakoid development, two slightly larger type 2 LHCII apoproteins of 28.3 and 28.7 kD also accumulate in thylakoids.
During the most rapid phase of thylakoid development (8-24 h), two slightly larger (28.3 and 28.7 kD) type 2 LHCII apoproteins (precursor intermediates?) also accumulate in the thylakoids
molecular mass 28.3 kDmolecular mass 28.7 kDtime window 8-24 h
Type 1, type 2, and type 3 LHCII apoproteins appear sooner in thylakoids from apical leaf segments than from basal leaf segments during greening.
appear somewhat sooner (< 4 h) in thylakoids from apical than from basal (4-8 h) leaf segments
appearance time 4 happearance time 4-8 h
Type 1, type 2, and type 3 LHCII apoproteins appear sooner in thylakoids from apical leaf segments than from basal leaf segments during greening.
appear somewhat sooner (< 4 h) in thylakoids from apical than from basal (4-8 h) leaf segments
appearance time 4 happearance time 4-8 h
Type 1, type 2, and type 3 LHCII apoproteins appear sooner in thylakoids from apical leaf segments than from basal leaf segments during greening.
appear somewhat sooner (< 4 h) in thylakoids from apical than from basal (4-8 h) leaf segments
appearance time 4 happearance time 4-8 h
Type 1, type 2, and type 3 LHCII apoproteins appear sooner in thylakoids from apical leaf segments than from basal leaf segments during greening.
appear somewhat sooner (< 4 h) in thylakoids from apical than from basal (4-8 h) leaf segments
appearance time 4 happearance time 4-8 h
Type 1, type 2, and type 3 LHCII apoproteins appear sooner in thylakoids from apical leaf segments than from basal leaf segments during greening.
appear somewhat sooner (< 4 h) in thylakoids from apical than from basal (4-8 h) leaf segments
appearance time 4 happearance time 4-8 h
Type 1, type 2, and type 3 LHCII apoproteins appear sooner in thylakoids from apical leaf segments than from basal leaf segments during greening.
appear somewhat sooner (< 4 h) in thylakoids from apical than from basal (4-8 h) leaf segments
appearance time 4 happearance time 4-8 h
Type 1, type 2, and type 3 LHCII apoproteins appear sooner in thylakoids from apical leaf segments than from basal leaf segments during greening.
appear somewhat sooner (< 4 h) in thylakoids from apical than from basal (4-8 h) leaf segments
appearance time 4 happearance time 4-8 h
Type 1, type 2, and type 3 LHCII apoproteins appear sooner in thylakoids from apical leaf segments than from basal leaf segments during greening.
appear somewhat sooner (< 4 h) in thylakoids from apical than from basal (4-8 h) leaf segments
appearance time 4 happearance time 4-8 h
Type 1, type 2, and type 3 LHCII apoproteins appear sooner in thylakoids from apical leaf segments than from basal leaf segments during greening.
appear somewhat sooner (< 4 h) in thylakoids from apical than from basal (4-8 h) leaf segments
appearance time 4 happearance time 4-8 h
Type 1, type 2, and type 3 LHCII apoproteins appear sooner in thylakoids from apical leaf segments than from basal leaf segments during greening.
appear somewhat sooner (< 4 h) in thylakoids from apical than from basal (4-8 h) leaf segments
appearance time 4 happearance time 4-8 h
Type 1, type 2, and type 3 LHCII apoproteins appear sooner in thylakoids from apical leaf segments than from basal leaf segments during greening.
appear somewhat sooner (< 4 h) in thylakoids from apical than from basal (4-8 h) leaf segments
appearance time 4 happearance time 4-8 h
Type 1, type 2, and type 3 LHCII apoproteins appear sooner in thylakoids from apical leaf segments than from basal leaf segments during greening.
appear somewhat sooner (< 4 h) in thylakoids from apical than from basal (4-8 h) leaf segments
appearance time 4 happearance time 4-8 h
Type 1, type 2, and type 3 LHCII apoproteins appear sooner in thylakoids from apical leaf segments than from basal leaf segments during greening.
appear somewhat sooner (< 4 h) in thylakoids from apical than from basal (4-8 h) leaf segments
appearance time 4 happearance time 4-8 h
Type 1, type 2, and type 3 LHCII apoproteins appear sooner in thylakoids from apical leaf segments than from basal leaf segments during greening.
appear somewhat sooner (< 4 h) in thylakoids from apical than from basal (4-8 h) leaf segments
appearance time 4 happearance time 4-8 h
Approval Evidence
1 source1 linked approval claimfirst-pass slug native-green-gel-system
we have studied the light-induced assembly of chlorophyll-protein complexes with a native green gel system
Source:
complex composition differencesupports
Differences remain apparent in chlorophyll-protein complex composition between light-control plants and etiolated plants greened for 8 days.
differences are still apparent in the composition of chlorophyll-protein complexes of light-control plants and those of etiolated plants greened for 8 d
Source:
Comparisons
Source-backed strengths
The method was applied directly to light-induced greening and supported resolution of LHCII-related species in a native context. In the cited work, it showed that type 1, type 2, and type 3 LHCII apoproteins accumulated simultaneously and at similar rates, and no corresponding higher molecular mass forms of type 1 and type 3 LHCII apoproteins were detected.
Compared with CLARITY technology
native green gel system and CLARITY technology address a similar problem space.
Shared frame: same top-level item type; same primary input modality: light
Compared with Langendorff perfused heart electrical recordings
native green gel system and Langendorff perfused heart electrical recordings address a similar problem space.
Shared frame: same top-level item type; same primary input modality: light
Compared with plant transcriptome profiling
native green gel system and plant transcriptome profiling address a similar problem space.
Shared frame: same top-level item type; same primary input modality: light
Ranked Citations
- 1.