Purification and characterization of a soluble endopeptidase from rat bone.
Purification and characterization of a soluble endopeptidase from rat bone.
复制标题
大鼠骨中可溶性肽链内切酶的纯化和表征。
DOI：
10.1007/bf02555875
复制
发表时间：
1991
影响因子：
4.2
通讯作者：
Makinen,KK
中科院分区：
文献类型：
--
作者：
Bollen,AM;Makinen,KK
A soluble endopeptidase was purified from rat bone using ammonium sulphate precipitation followed by Fast Protein Liquid Chromatography on gel, anion exchange, and chromatofocusing columns. The enzyme was silver stain-pure (SDS-PAGE) and its apparent molecular weight was 60,000. In general, the enzyme favored the hydrolysis of the X-Y bond in substrates with the sequence of-Pro-X-Y-Pro-, where either X or Y (or both) were hydrophobic residues. The presence of imino acid residues near the scissile bond favored hydrolysis. The enzyme was strongly inactivated by metal chelating agents andp-hydroxymercuribenzoic acid, indicating that SH-groups may be necessary for full activity of the enyme and that the enzyme may be a metallopeptidase.
