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：1983
卷号：80
期号：4
页码：973-977
DOI：10.1073/pnas.80.4.973
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：Unlabeled prohistidine decarboxylase and prohistidine decarboxylase containing L-[carboxyl-18O]serine or L-[hydroxyl-18O]serine were isolated in homogeneous form from mutant 3 of Lactobacillus 30a grown with the appropriately labeled serine. There was no randomization or redistribution of label during growth, isolation of the protein, or enzymatic hydrolysis and reisolation of the labeled amino acids. These proteins were used to show that during proenzyme activation, in which individual {pi} subunits of the proenzyme are converted to and {beta} subunits of the active enzyme [Formula: see text] (in which {pi
