A study of human tissue aminopeptidase components.
A study of human tissue aminopeptidase components.
复制标题
人体组织氨肽酶成分的研究。
DOI:
10.1016/0003-9861(65)90194-3
复制
发表时间:
1965
影响因子:
3.9
通讯作者:
J. Hardman
中科院分区:
文献类型:
--
作者:
F. J. Běhal;B. Asserson;F. Dawson;J. Hardman
The aminopeptidase activity of human liver, small intestine, and pancreas was studied. Liver contained two chromatographically resolvable types of aminopeptidase, one Mn++-dependent and active on dipeptides and a second with no metal ion requirement and active on amino acid β-naphthylamides (BNA). Intestine contained a Mn++-dependent aminopeptidase active on dipeptides and a Co++-dependent aminopeptidase active on amino acid BNA which eluted simultaneously from a column. Pancreas also contained both types of aminopeptidase activity; the activity on amino acid BNA, Co++-dependent, was chromatographically resolved into two components. In all cases aminopeptidase activity on dipeptides was insensitive to puromycin while aminopeptidase activity on amino acid BNA was quite sensitive to puromycin.