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J. Biochem, 1982, Vol. 91, No. 4 1129-1137
© 1982 Japanese Biochemical Society

research-article

Purification of RNA Associated and Unassociated Forms of 1,4-{alpha}-Glucan Branching Enzyme from Rat Liver1

Kimihiko SATOH and Kiyomi SATO2

Second Department of Biochemistry, Hirosaki University School of Medicine Hirosaki, Aomori 036

Two molecular forms (BE-I and -II) of 1,4-a-glucan branching enzyme were purified from rat liver by affinity chromatography on glycogen-adipoyldihydrazide-Sepharose 4B and glycogen-ethylenediamine-Sepharose 4B, respectively, after hydrophobic chromatography on hexylamine-Sepharose 4B, as single proteins with the same molecular weight of 82,000 on SDS-polyacrylamide gel electrophoresis. By comparing their UV spectra and by RNA detection on polyacrylamide gels after electrophoresis, BE-I and -II were identified to be RNA associated and unassociated forms, respectively. The molecular weights of BE-I and -II estimated by Sephadex G-200 gel filtration were 91,000 and 98,000, respectively, indicating that both forms consist of a monomer. As BE-II had about half the specific activity of BE-I, the RNA component was not essential for the activity of the rat liver branching enzyme, and it was also dissociable from the protein component (BE-II) on polyacrylamide gel electrophoresis at pH 7.3, whereby BE-II showed a heterogeneity of at least three microspecies as revealed by protein staining as well as by activity staining of the gels. Using the antibody against BE-I, BE-I and -II were indistinguishable on immuno-diffusion, and the activity inhibition rate of BE-II by the antibody was almost the same as that of BE-I if their specific activities are considered, indicating that the RNA component may have no effect on the enzyme-antibody reaction. Immuno-chemically no isoenzyme was detected for this enzyme in rat tissues.

1This study was supported in part by Grants-in-Aid from the Ministry of Education, Science and Culture of Japan.

2To whom requests for reprints should be addressed.


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