alpha-Glucan synthesis on a protein primer, uridine diphosphoglucose: protein transglucosylase I. Separation from starch synthetase and phosphorylase and a study of its properties.
作者： Silvia MORENO , Carlos E. CARDINI , Juana S. TANDECARZ
DOI: 10.1111/J.1432-1033.1986.TB09700.X
关键词:
摘要: It was found that the DEAE-cellulose-treated UDP-Glc:protein transglucosylase I catalyzing first step (reaction 1) in formation of α-glucan bound to protein potato tuber is not only specific for glucosyl donor but also endogenous acceptor. A single radioactive 38-kDa macromolecular component appeared during denaturing polyacrylamide gel electrophoresis reaction 1 product. The labeled probably polypeptide subunit acceptor which being glucosylated. radioactivity incorporated product isolated from a protease digest as low-molecular-mass glucopeptide fraction. β-elimination carried out presence reducing agent demonstrated one moiety transferred UDP-Glc aminoacyl residue, thus forming an O-glucosidic linkage. 3H-labeled sodium borohydride showed serine and threonine are involved peptide bond glucose. Ion-exchange chromatography on DEAE-cellulose, affinity concanavalin-A—Sepharose, filtration Sephacryl S-300 sucrose density gradient centrifugation failed separate enzyme
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