SOLUBLE EXOPEPTIDASES OF BOVINE AND HUMAN LENS - CHARACTERIZATION BY ELECTROPHORESIS
SOLUBLE EXOPEPTIDASES OF BOVINE AND HUMAN LENS - CHARACTERIZATION BY ELECTROPHORESIS
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DOI：
10.3109/02713688409011748
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发表时间：
1984-01-01
影响因子：
2
通讯作者：
HARRIS, H
中科院分区：
文献类型：
--
作者：
LAFFERTY, MA;RADUCHA, M;HARRIS, H
可溶性外肽酶存在于牛和人的晶状体进行了鉴定和表征，使用淀粉凝胶电泳分离，然后用L-氨基酸氧化酶/过氧化物酶系统或萘胺荧光系统的活性染色。使用肽（16）和萘酰胺底物（12）。测定了每种分离的外肽酶的底物特异性谱。表征还包括pH、EDTA、嘌呤霉素和二价阳离子对活性的影响。通过凝胶过滤进行MW测定。鉴定了6种牛透镜肽酶，包括亮氨酸氨肽酶和二肽基肽酶III，以及6种人透镜肽酶，包括二肽基肽酶III。牛亮氨酸氨肽酶与以前命名为肽酶S的一种人肽酶之间在底物特异性和分子量方面具有很强的同源性。这些发现表明透镜中可用于多肽降解的外肽酶的多样性。
Soluble exopeptidases present in bovine and human lenses were identified and characterized using starch gel electrophoresis separation followed by activity staining with an L-amino acid oxidase/peroxidase system or a naphthylamine fluorescence system. Peptide (16) and naphthylamide substrates (12) were used. The profile of substrate specificities for each electrophoretically separated exopeptidase was determined. Characterization also included the effects on activity of pH, EDTA, puromycin and divalent cations. MW determinations by gel filtration were made. Six bovine lens peptidases were identified including leucine aminopeptidase and dipeptidylpeptidase III and 6 human lens peptidases including dipeptidylpeptidase III. Strong homology in terms of substrate specificity and MW was seen between bovine leucine aminopeptidase and 1 of the human peptidases previously designated peptidase S. The findings indicate the diversity of exopeptidases available for polypeptide degradation in lens.