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：1980
卷号：77
期号：6
页码：3669-3671
DOI：10.1073/pnas.77.6.3669
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：The brain cholecystokinin-converting enzymes that cleave intact cholecystokinin to its COOH-terminal dodecapeptide and octapeptide also cleave the synthetic dipeptides Arg-Ile (or Arg-Val or Arg-Leu) and Arg-Asp, respectively. Thus, they are not hormone-specific enzymes but are bond-specific. Ultracentrifuge studies demonstrate that there is Arg-Ile hydrolase activity associated with a protein greater in molecular weight than gamma globulin and that both Arg-Ile and Arg-Asp hydrolase activities are associated with one or more proteins between albumin and gamma globulin in molecular weight.
