Purification and characterization of the main pepsinogen from the shark, Centroscymnus coelolepis
Purification and characterization of the main pepsinogen from the shark, Centroscymnus coelolepis
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DOI：
10.1093/oxfordjournals.jbchem.a022109
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发表时间：
1998-08-01
影响因子：
2.7
通讯作者：
Léonil, J
中科院分区：
文献类型：
--
作者：
Nguyen, AD;Nungaray, J;Léonil, J
从鲨鱼（Centroscymnus coelolepis）粘膜中提取的主要胃蛋白酶原已被纯化和鉴定。这种酶原，在数量和活性方面最丰富的蛋白质（产率72%），是一种分子量为42 +/-0.7kDa的均相单体，通过电泳测定。这种酶的胆固醇基蛋白酶性质通过胃蛋白酶抑制剂的显著抑制而得到证实，采用电喷雾质谱法（ESI-MS）测定了其对牛胰岛素氧化B链的特异性与反相高压液相色谱（RP-HPLC）联用。15-16 Leu-Tyr键在该底物中迅速裂解，随后是24-25 Phe-Phe、25-26 Phe-Tyr和11-12 Leu-Val键。
The main pepsinogen from the mucosa of the shark, Centroscymnus coelolepis, has been purified and characterized. This zymogen, the most abundant protein in terms of quantity and activity (yield 72%), is a homogeneous monomer of molecular weight 42 +/- 0.7 kDa, as determined by electrophoresis, The aspartyl proteinase nature of this enzyme was confirmed by the considerable inhibition by pepstatin, Its specificity as to the oxidized B-chain of bovine insulin was determined using electrospray ionization mass spectrometry (ESI-MS) coupled with reversed phase high pressure liquid chromatography (RP-HPLC). The 15-16 Leu-Tyr bond was rapidly cleaved in this substrate, followed by the 24-25 Phe-Phe, 25-26 Phe-Tyr, and 11-12 Leu-Val bonds.