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：1976
卷号：73
期号：1
页码：77-81
DOI：10.1073/pnas.73.1.77
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：Highly purified platelet glucose-6-phosphate dehydrogenase (G6PD; D-glucose-6-phosphate:NADP+ 1-oxidoreductase, EC 1.1.1.49 ) can be modified in its isoelectric point and its molecular specific activity by extracts of some leukemic granulocytes. The "G6PD modifying factors" are relatively small molecules (molecular weight slightly under 5000), thermostable, dialyzable, and ultrafilterable. These molecules are destroyed by various endo- and exopeptidases and by serine enzymes present in crude extracts of leukocytes and commercial preparations of ribonuclease. The alterations of platelet G6PD due to the "G6PD modifying factors" are stable and not reversible by dialysis or further chromatography. The leukemic extracts which are able to modify G6PD also can modify the electrophoretic mobility and (or) the enzymatic activity of purified leukocyte pyruvate kinase, 6-phosphogluconate dehydrogenase, and glucosephosphate isomerase. The chemical nature of such modifications and their relationships with post-translational modifications which occur in leukemic or normal cells are discussed.
