A 36 kDa calcium/phospholipid binding protein in human placenta was identified as VAC-beta (annexin-8)
First-pass extracted concept
VAC-beta (annexin-8)
Aliases
annexin-8, VAC-beta
Evidence Snippets
Supporting Sources
Linked Claims
Annexin-8 is a minor product in human placenta, accounting for less than 1% of extracted annexins.
The protein is a minor product in placenta, accounting for less than 1% of extracted annexins.
By anion-exchange chromatography on diethylaminoethyl-cellulose, annexin-8 coeluted with annexin-3.
By anion-exchange chromatography on diethylaminoethyl-cellulose annexin-8 coeluted with annexin-3.
The authors propose that annexin-8 being a minor component in standard annexin preparations and co-eluting with annexin-3 by ion exchange chromatography likely explain why other labs failed to characterize it.
The combination of annexin-8 being a minor component in standard annexin preparations and it co-eluting with annexin-3 by ion exchange chromatography are likely to account for the failure of other labs to characterize the product.
A 36 kDa calcium/phospholipid binding protein in human placenta was identified as VAC-beta (annexin-8).
A 36 kDa calcium/phospholipid binding protein in human placenta was identified as VAC-beta (annexin-8) by a combination of immunological and peptide mapping analyses.
By gel filtration, annexin-8 eluted as a broad peak with approximately half as monomer and half as a heterodimer associated with a 10 kDa subunit.
By gel filtration, the protein chromatographed as a broad peak, where half the product eluted as a monomer and half eluted as a heterodimer that was associated with a 10 kDa subunit.
From 150 g of placenta tissue, only 100 micrograms of annexin-8 was isolated.
From 150 g of tissue, only 100 micrograms of the protein was isolated.