Barrett A J, Tisljar U
Department of Biochemistry, Strangeways Research Laboratory, Cambridge, U.K.
Biochem J. 1989 Aug 1;261(3):1047-50. doi: 10.1042/bj2611047.
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.
研究发现，Pz肽酶（用2,4 - 二硝基苯基 - Pro - Leu - Gly - Pro - Trp - D - Lys测定）和内肽酶24.15（用苯甲酰 - Gly - Ala - Ala - Phe - 对氨基苯甲酸测定）是从大鼠骨骼肌中共纯化得到的，在高分辨率凝胶色谱中共同洗脱，并且共存于大鼠睾丸内肽酶24.15的纯化物中。大鼠睾丸中部分纯化的Pz肽酶对4 - 苯基偶氮苄氧基羰基 - Pro - Leu - Gly - Pro - D - Arg的作用被内肽酶24.15的抑制剂以及该酶的一种底物所阻断。部分纯化的该酶水解内肽酶24.15的两种底物，其米氏常数与先前发表的相似，并且其对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特异性的化合物所抑制。我们得出结论，先前归因于两种不同酶的活性仅由一种酶引起，并且这两篇文献的合并可能会引发新的研究方向。
