Further purification and some properties of a gelatin-specific proteinase of human leucocytes.
Further purification and some properties of a gelatin-specific proteinase of human leucocytes.
复制标题
人白细胞明胶特异性蛋白酶的进一步纯化和一些特性。
DOI：
10.1016/0304-4165(82)90375-0
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发表时间：
1982
期刊：
影响因子：
--
通讯作者：
I. Sopata
中科院分区：
文献类型：
--
作者：
I. Sopata
从人白细胞的粗提物中分离出一种潜在的明胶特异性蛋白酶（明胶酶）。该酶纯化约 180 倍（7040 单位/毫克），总产率为 23%。分离的蛋白质在十二烷基硫酸钠聚丙烯酰胺凝胶电泳上迁移为单条带。其流动性不受还原剂影响。蛋白质条带对应于大约。 90–94 kDa。明胶酶活性受到螯合剂（例如 EDTA 和 1,10-菲咯啉）的强烈抑制。这种抑制作用可被 Zn2+ 和 Co2+ 逆转；其他金属离子在逆转抑制方面效果较差或根本无效。此外，Co2+ 刺激明胶酶活性。这些结果表明 Zn2+ 和/或 Co2+ 对于该明胶酶的活性至关重要。
A latent gelatin-specific proteinase (gelatinase) was isolated from the crude extract of human leukocytes. The enzyme was purified about 180-fold (7040 units/mg) with an overall yield of 23%. The isolated protein migrated as a single band on sodium dodecyl sulfate polyacrylamide-gel electrophoresis. Its mobility was unaffected by reducing agent. The protein band corresponded to approx. 90–94 kDa. Gelatinase activity was strongly inhibited by chelating agents, such as EDTA and 1,10-phenanthroline. This inhibition was reversed by Zn2+and Co2+; other metal ions were less or not at all effective in reversing the inhibition. Moreover, Co2+stimulated gelatinase activity. These results indicate that Zn2+and/or Co2+are essential for the activity of this gelatinase.
人皮肤明胶特异性中性蛋白酶的纯化和特性。
DOI：
--
发表时间：
1981
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Seltzer,JL;Adams,SA;Grant,GA;Eisen,AZ
通讯作者：
Eisen,AZ