期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1974
卷号：71
期号：5
页码：1701-1704
DOI：10.1073/pnas.71.5.1701
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：Protein carboxymethylase, an enzyme capable of methylating proteins and polypeptides, was purified from bovine pituitary. The anterior pituitary hormones, luteinizing hormone, follicle-stimulating hormone, adrenocorticotropic hormone, growth hormone, thyroid-stimulating hormone, and prolactin, were found to be substrates for this enzyme. The posterior pituitary hormones, oxytocin and vasopressin, did not serve as substrates. With luteinizing hormone as the substrate, protein carboxymethylase had a pH optimum near pH 5.5. A limiting Km of 1.47 {micro}M for S-adenosyl-L-methionine was obtained with luteinizing hormone as the methyl acceptor. Possible roles of this enzyme in the posterior and anterior pituitary are discussed.
关键词：protein hormones ; S -adenosyl-L-methionine ; neuroendocrine ; methanol-forming enzyme
