Norén O, Sjöström H, Danielsen E M, Staun M, Jeppesen L, Svensson B
Hoppe Seylers Z Physiol Chem. 1979 Feb;360(2):151-7. doi: 10.1515/bchm2.1979.360.1.151.
Intestinal dipeptidyl peptidase IV and gamma-glutamyltransferase were compared to the corresponding kidney enzymes with respect to immunological and electrophoretic properties. The influences of selected effectors on the two enzymes were also studied. The two kidney peptidases exhibited the reaction of total identity with the corresponding intestinal enzymes in immunodiffusion. Furthermore, the intestinal dipeptidyl peptidase IV and gamma-glutamyl transferase showed the same inhibition patterns as the corresponding kidney enzymes and the acceptor specificity of the intestinal gamma-glutamyl-transferase was found to be identical to that of the kidney enzyme. The electrophoretic mobilities of dipeptidyl peptidase IV from the two organs differed greatly. The difference was almost abolished by treatment with neuraminidase, suggesting that the variation in mobility was due to different contents of sialic acid. It is suggested that the intestinal brush border peptidases, dipeptidyl peptidase IV and gamma-glutamyltransferase, are closely related to the corresponding enzymes obtained from the kidney.
就免疫和电泳特性而言,对肠二肽基肽酶IV和γ-谷氨酰转移酶与相应的肾酶进行了比较。还研究了选定效应物对这两种酶的影响。两种肾肽酶在免疫扩散中与相应的肠酶表现出完全相同的反应。此外,肠二肽基肽酶IV和γ-谷氨酰转移酶显示出与相应肾酶相同的抑制模式,并且发现肠γ-谷氨酰转移酶的受体特异性与肾酶相同。来自两个器官的二肽基肽酶IV的电泳迁移率差异很大。用神经氨酸酶处理后这种差异几乎消失,表明迁移率的变化是由于唾液酸含量不同。提示肠刷状缘肽酶,即二肽基肽酶IV和γ-谷氨酰转移酶,与从肾脏获得的相应酶密切相关。