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Polyacrylamide gradient gel electrophoresis of cytosolic aretinol‐ and retinoic acid‐binding proteins: Application to rat testis and liver
Author(s) -
Melin AnneMarie,
Carbonneau MarieAnnette,
Maviel MarieJosée,
Clerc Michel
Publication year - 1989
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.1150101107
Subject(s) - retinoic acid , polyacrylamide gel electrophoresis , cytosol , gel electrophoresis , electrophoresis , gel electrophoresis of proteins , retinol binding protein , polyacrylamide , molecular weight size marker , biochemistry , binding protein , chemistry , chromatography , microbiology and biotechnology , biology , retinol , enzyme , gene , vitamin
Distribution and cellular levels of retinol‐binding protein and retinoic acid‐binding protein, involved in the molecular action of retinoids, were analyzed in rat testis and liver. Both binding proteins of cytosolic extracts were separated by linear‐polyacryl‐amide gradient gel electrophoresis and following electrophoretic separation, could be visualized by complementary identification tests such as autoradiography and marker proteins. The concentrations of the binding proteins were evaluated by scanning the polyacrylamide gradient gels and the resulting data were found to be in accordance with those obtained by counting radioactivities. Polyacrylamide gradient gel electrophoresis appears suitable to detect and quantitatively evaluate cytosolic retinol‐ and retinoic acid‐binding proteins.