Activity of Pz-peptidase and endo-oligopeptidase are due to the same enzyme.
Activity of Pz-peptidase and endo-oligopeptidase are due to the same enzyme.
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Pz-肽酶和内切寡肽酶的活性归因于相同的酶。
DOI：
10.1016/0006-291x(89)90838-3
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发表时间：
1989
影响因子：
3.1
通讯作者：
A. Barrett
中科院分区：
文献类型：
--
作者：
U. Tisljar;A. C. D. de Camargo;C. A. da Costa;A. Barrett
在兔心脏内寡肽酶的纯化过程中，在相同的组分中发现了切割内寡肽酶底物缓激肽和Pz-肽酶底物Mcc-Pro-Leu-gly-Pro-D-LyS（Dnp）的活性。这两种底物的水解都被内寡肽酶和Pz-肽酶的抗血清所抑制，并被1，10-菲咯啉可逆地抑制。纯化的酶水解Pz-肽酶的另一底物Dnp-Pro-Leu-Gly-Pro-Trp-D-Lys。从兔肌肉中纯化的Pz-肽酶降解缓激肽，并被抗内寡肽酶的抗血清抑制。
During purification of endo-oligopeptidase from rabbit heart, activities cleaving bradykinin, a substrate of endo-oligo-peptidase, and Mcc-Pro-Leu-gly-Pro-D-Lys(Dnp), a substrate of Pz-peptidase, were found in the same fractions. The hydrolysis of both substrates was inhibited by antisera against endo-oligo-peptidase and Pz-peptidase, and reversibly inhibited by 1, 10-phenanthroline. The purified enzyme hydrolysed Dnp-Pro-Leu-Gly-Pro-Trp-D-Lys, another substrate of Pz-peptidase. Purified Pz-peptidase from rabbit muscle degraded bradykinin and was inhibited by an antiserum against endo-oligopeptidase.