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On a basic 31 kDa muscle membrane protein in cattle and pig, presumably equivalent to the class II antigen associated p31 molecule
Author(s) -
Thinnes Friedrich Peter,
Meyer Anke,
Schwartzenberg Klaus
Publication year - 1984
Publication title -
animal blood groups and biochemical genetics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.756
H-Index - 81
eISSN - 1365-2052
pISSN - 0003-3480
DOI - 10.1111/j.1365-2052.1984.tb01115.x
Subject(s) - isoelectric point , antigen , biology , isoelectric focusing , glycoprotein , microbiology and biotechnology , membrane , membrane protein , gel electrophoresis , molecular mass , biochemistry , genetics , enzyme
Summary In a recent paper we gave evidence by two‐dimensional electrophoresis that, in man, the class II antigen associated glycoprotein p31 (also called Ii, In, M1, DRγ, XMl) is expressed not only in the membranes of B lymphocytes but also in those of muscle, liver and brain. It can therefore be assumed that the p31 is not really associated with the human class II antigens but is a ubiquitous molecule. Here we demonstrate for the first time that the muscle membranes of cattle and pig contain corresponding polypeptides, with a molecular weight of about 31 kDa and an isoelectric point around 7.5, which comigrate in two‐dimensional electrophoresis with p31 derived from the human muscle. Thus, in cattle and pig too, these proteins seem to be equivalent to the class II antigen associated p31, showing a tissue distribution wider than observed up to now. The molecules can be concentrated by ion‐exchange chromatography.