EVOLUTIONARY ORIGIN OF THE PHYSIOLOGICAL LIGAND BINDING SPECIFICITY OF SERUM ALBUMIN - THE ALLOSTERIC DOMAIN MODEL

Authors
  1. Hsia, J.C.
Corporate Authors
Defence and Civil Inst of Environmental Medicine, Downsview ONT (CAN)
Abstract
Results from spin label studies of human serum albumin binding specificities and mechanisms and their clinical implications are reviewed. Bilirubin, palmitate and octanoate have been shown to bind to six mono-anionic ligand binding sites, occurring in pairs and allosterically linked on albumin. The evolutionary origin of these anionic ligand binding sites and a functional allosteric domain model are described.
Report Number
80-P-47 — Conference Paper
Date of publication
01 Jan 1981
Number of Pages
6
Reprinted from
Periodicum Biologorum, vol 83, no 1, 1981, p 99-104
DSTKIM No
82-03209
CANDIS No
37582
Format(s):
Hardcopy;Originator's fiche received by DSIS

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