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Binding of galactosylsphingosine (psychosine) by albumin
Author(s) -
Igisu Hideki,
Matsuoka Masato,
Hamasaki Naotaka
Publication year - 1990
Publication title -
lipids
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.601
H-Index - 120
eISSN - 1558-9307
pISSN - 0024-4201
DOI - 10.1007/bf02562430
Subject(s) - albumin , chromatography , sephadex , chemistry , size exclusion chromatography , serum albumin , dissociation constant , biochemistry , enzyme , receptor
Abstract On applying [ 3 H]galactosylsphingosine (psychosine) and albumin to a gel filtration column, either as a pre‐incubated mixture or as separate solutions, the lipid and albumin co‐eluted. When albumin and [ 3 H]galactosylsphingosine were incubated with Sephadex G‐50, the concentration of galactosylsphingosine outside the gel increased as the concentration of albumin increased. These observations indicate that albumin binds galactosylsphingosine. By using an equilibrium gel procedure, it was estimated that one molecule of albumin has 7.4 binding sites for galactosylsphingosine, and that the dissociation constant is 3.9×10 −6 M. These values appear compatible with the potency of albumin to suppress galactosylsphingosine‐induced hemolysis.