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首页> 外文期刊>Biochemical Pharmacology >A kinetic study of glucagon-like peptide-1 and glucagon-like peptide-2 truncation by dipeptidyl peptidase IV, in vitro.
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A kinetic study of glucagon-like peptide-1 and glucagon-like peptide-2 truncation by dipeptidyl peptidase IV, in vitro.

机译:在体外通过二肽基肽酶IV截断胰高血糖素样肽-1和胰高血糖素样肽2的动力学研究。

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摘要

In vivo inactivation of glucagon-like peptide-1 (GLP-1) and glucagon-like peptide-2 (GLP-2) was found to be associated with the proteolytic removal of their N-terminal dipeptide by the ectopeptidase dipeptidyl peptidase IV (DPP IV). Previous studies suggested that the in vivo metabolism of GLP-1 is much faster than that of GLP-2. In this paper, we investigated the in vitro truncation of GLP-2 and GLP-1 by DPP IV. The slower conversion rate observed for GLP-2 compared to GLP-1 was due to an approximately 10-fold reduction in catalytic rate constant. The selectivity of DPP IV for the glucagon-like peptides was compared with data obtained for other natural substrates using the same enzyme source in identical conditions.
机译:发现体内胰高血糖素样肽-1(GLP-1)和胰高血糖素样肽2(GLP-2)的失活与通过肽肽酶二肽基肽酶IV(DPP)的N端二肽蛋白水解去除有关。 IV)。先前的研究表明,GLP-1的体内代谢比GLP-2快得多。在本文中,我们研究了DPP IV在体外截短GLP-2和GLP-1的方法。与GLP-1相比,GLP-2的转化率较慢是由于催化速率常数降低了约10倍。将DPP IV对胰高血糖素样肽的选择性与在相同条件下使用相同酶源获得的其他天然底物的数据进行了比较。

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