链霉菌属产生的碱性丝氨酸蛋白酶可降解PrP(Sc)。
Alkaline serine protease produced by Streptomyces sp. degrades PrP(Sc).
作者信息
Hui Zhao, Doi Hiroyasu, Kanouchi Hiroaki, Matsuura Yuichi, Mohri Shiro, Nonomura Yoshiaki, Oka Tatsuzo
机构信息
Department of Veterinary Physiology, Faculty of Agriculture, Kagoshima University, Kagoshima 890-0065, Japan.
出版信息
Biochem Biophys Res Commun. 2004 Aug 13;321(1):45-50. doi: 10.1016/j.bbrc.2004.06.100.
A PrP(Sc)-degrading enzyme was isolated from the culture medium of Streptomyces sp. using perchloric acid-soluble protein (PSP) as a substrate. The media of 500 microbial species were screened to obtain the PSP-degrading enzyme. The medium containing the protease secreted from strain 99-GP-2D-5 showed the highest PSP-degrading activity. Strain 99-GP-2D-5 was assigned as the genus Streptomyces by its morphological and chemotaxonomic characteristics. When scrapie prion was used as the substrate, it was completely digested by the enzyme. The amino acid sequence of the enzyme was identical to that of the C-terminal region of alkaline serine protease (ASP) I. ASP I may be the precursor of the enzyme, and the enzyme seems to be the mature type of ASP I. The maximal activity of the enzyme was observed at 60 degrees C and pH 11, and the scrapie prion was degraded within 3 min under the optimum conditions.
以高氯酸可溶性蛋白（PSP）为底物，从链霉菌属的培养基中分离出一种PrP(Sc)降解酶。筛选了500种微生物的培养基以获得PSP降解酶。含有菌株99-GP-2D-5分泌的蛋白酶的培养基显示出最高的PSP降解活性。根据其形态学和化学分类学特征，菌株99-GP-2D-5被归为链霉菌属。当以羊瘙痒病朊病毒为底物时，该酶可将其完全消化。该酶的氨基酸序列与碱性丝氨酸蛋白酶（ASP）I的C末端区域相同。ASP I可能是该酶的前体，而该酶似乎是ASP I的成熟类型。该酶在60℃和pH 11时观察到最大活性，在最佳条件下，羊瘙痒病朊病毒在3分钟内被降解。
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