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Palmitate‐binding, serum albumin‐like proteins in salmonids
Author(s) -
Davidson William S.,
Birt Victoria L.,
Birt Tim P.,
Green John M.
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)80446-0
Subject(s) - albumin , polyacrylamide gel electrophoresis , biochemistry , serum albumin , bovine serum albumin , blood proteins , molecular mass , electrophoresis , chemistry , plasma protein binding , gel electrophoresis , homologous chromosome , fish <actinopterygii> , biology , fishery , gene , enzyme
There has been considerable controversy over the existence of serum albumin in fish. One of the physiological functions of albumin is to bind free fatty acids. This characteristic was used to screen the plasma of seven species of salmonids. Each species contains a protein fraction that (i) binds palmitate, (ii) has a molecular mass similar to that of human serum albumin, and (iii) is one of the most rapidly migrating proteins when salmonid plasma is subjected to anodal polyacrylamide gel electrophoresis. We conclude therefore, that salmonids have serum albumins that are homologous to the serum albumin of higher vertebrates.