Bilirubin binding by the fractionated alternate allelic components of heterozygous monkey albumin

Analysis of bilirubin‐binding parameters for purified albumin of nine rhesus monkeys heterozygous for albumin MacA and albumin MacB was performed after separating these two albumin forms by fast protein liquid chromatography (FPLC). The binding capacity (n) for MacA‐enriched samples was lower than t...

Full description

Saved in:
Bibliographic Details
Published in:American journal of physical anthropology 1985-10, Vol.68 (2), p.169-171
Main Authors: Lorey, Fred W., Smith, David G., Ahlfors, Charles E.
Format: Article
Language:English
Subjects:
albumin
Albumin polymorphisms
Alleles
Animals
Bilirubin
Bilirubin - blood
Binding capacity affinity
FPLC
Heterozygote
Macaca mulatta
Serum Albumin - genetics
Serum Albumin - isolation & purification
Serum Albumin - metabolism
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Analysis of bilirubin‐binding parameters for purified albumin of nine rhesus monkeys heterozygous for albumin MacA and albumin MacB was performed after separating these two albumin forms by fast protein liquid chromatography (FPLC). The binding capacity (n) for MacA‐enriched samples was lower than that for the MacB variant in eight of nine fraction pairs analyzed, while the affinity constant (K) was higher in all nine MacA‐enriched samples. The values for n × K were higher in MacA‐enriched samples in eight of nine pairs tested. These data, together with previous studies, geographic specificity of the MacB variant, and the presence of dietary competitors for the primary bilirubin binding site on the albumin molecule, suggest an evolutionary advantage for the MacB variant only in areas where the dietary competitors are present.
ISSN:0002-9483
1096-8644
DOI:10.1002/ajpa.1330680204