The activities of 'Pz-peptidase' and 'endopeptidase 24.15' are due to a single enzyme.
The activities of 'Pz-peptidase' and 'endopeptidase 24.15' are due to a single enzyme.
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“Pz-肽酶”和“内肽酶 24.15”的活性归因于单一酶。
DOI：
10.1042/bj2611047
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发表时间：
1989
期刊：
影响因子：
--
通讯作者：
U. Tisljar
中科院分区：
文献类型：
--
作者：
A. Barrett;U. Tisljar
2，4-二硝基苯基-Pro-亮氨酸-甘氨酸-Pro-Trp-D-Lys测定的PZ-多肽酶和苯甲酰-甘氨酸-丙氨酸-丙氨酸-苯丙氨酸-对氨基苯甲酸测定的内肽酶24.15是从大鼠骨骼肌中共纯化的，它们在高分辨凝胶层析中共洗脱，并共存于大鼠睾丸内肽酶24.15的均一制剂中。部分纯化的大鼠睾丸PZ-肽酶对4-phenylazobenzyloxycarbonyl-Pro-Leu-Gly-Pro-D-Arg的作用可被内肽酶抑制剂24.15和该酶的底物阻断。该部分纯化的酶对内肽酶24.15的两种底物的Km值与先前报道的相似，其对2，4-二硝基苯基-Pro-Leu-Gly-Pro-Trp-D-Lys的作用被认为是内肽酶24.15专一性的化合物所抑制。我们的结论是，以前归因于两种不同酶的活性只归因于一种酶，这两篇文献的合并可能会带来新的研究思路。
It was found that Pz-peptidase (assayed with 2,4-dinitrophenyl-Pro-Leu-Gly-Pro-Trp-D-Lys) and endopeptidase 24.15 (assayed with benzoyl-Gly-Ala-Ala-Phe-p-aminobenzoate) were co-purified from rat skeletal muscle, were co-eluted in high-resolution gel chromatography and co-existed in a homogeneous preparation of rat testis endopeptidase 24.15. The action of partially purified Pz-peptidase from rat testis on 4-phenylazobenzyloxycarbonyl-Pro-Leu-Gly-Pro-D-Arg was blocked by an inhibitor of endopeptidase 24.15, and also by a substrate of this enzyme. The partially purified enzyme hydrolysed two substrates of endopeptidase 24.15 with Km values similar to those published previously, and its action on 2,4-dinitrophenyl-Pro-Leu-Gly-Pro-Trp-D-Lys was inhibited by compounds that are considered specific for endopeptidase 24.15. We conclude that the activities previously attributed to two distinct enzymes are due to only one, and that the merging of the two literatures may lead to new lines of research.