Premium
Acrylamide Electrophoresis and Binding Ability of Hepatic Ribosomal Protein from Normal and from Diabetic Rats
Author(s) -
Tragi K. H.,
Reaven G. M.
Publication year - 1973
Publication title -
european journal of clinical investigation
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.164
H-Index - 107
eISSN - 1365-2362
pISSN - 0014-2972
DOI - 10.1111/j.1365-2362.1973.tb00326.x
Subject(s) - ribosome , alloxan , ribosomal rna , diabetes mellitus , polyacrylamide gel electrophoresis , ribosomal protein , biochemistry , messenger rna , insulin , protein biosynthesis , rna , gel electrophoresis , biology , chemistry , endocrinology , medicine , enzyme , gene
Abstract. Liver ribosomes were isolated from normal and diabetic rats. Diabetes mellitus was induced either by the administration of alloxan or by injection of anti‐insulin serum. Treatment of rat liver ribosomes with ammonium chloride leads to a detachment of proteins which have an inhibitory effect on the binding of polyuridylic acid (poly U) to ribosomes. However, there is evidence that these proteins do bind to poly U and that there is less binding of proteins derived from diabetic liver ribosomes than of proteins derived from normal animals. The separation of these detachable proteins by means of a polyacrylamide gel electrophoresis reveals a quantitative increase of one single protein. The appearance of this increase is independent of the mode of induction of diabetes (alloxan, anti‐insulin serum) and is abolished by the administration of insulin. This finding added to the evidence of a reduction of ribosomal aggregation in diabetes mellitus could lead one to suggest the hypothesis that this detachable ribosomal protein has a repressive function with regard to the binding of messenger RNA to the ribosome.