Open AccessIsolation from Trout Liver of a Methionine‐Containing H1 Subfraction, THI met
Author(s) -
BROWN Elizabeth,
GOODWIN Graham H.
Publication year - 1983
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1983.tb07559.x
Subject(s) - cyanogen bromide , methionine , trout , cleavage (geology) , residue (chemistry) , chemistry , amino acid , rainbow trout , polyacrylamide gel electrophoresis , biochemistry , chromatography , biology , peptide sequence , fish <actinopterygii> , enzyme , fishery , paleontology , fracture (geology) , gene
A trout H1 subfraction, THI met , which contains one residue of methionine and has a blocked N‐terminal amino acid, has been isolated from trout liver. Cyanogen bromide cleavage of THI met and amino acid analysis and polyacrylamide gel electrophoresis of the cleavage products show that it contains a residue of methionine at about the same distance from the N terminus as mammalian H1° and avian H5. THI met is shown to be similar to, but not identical with, the protein derived from trout erythrocytes generally accepted as the equivalent in fish of avian H5.