牛组织蛋白酶S的一级结构。与组织蛋白酶L、H、B及木瓜蛋白酶的比较。

Primary structure of bovine cathepsin S. Comparison to cathepsins L, H, B and papain.

作者信息

Wiederanders B, Broemme D, Kirschke H, Kalkkinen N, Rinne A, Paquette T, Toothman P

机构信息

Institute of Biochemistry, Faculty of Medicine, University of Halle, Germany.

出版信息

FEBS Lett. 1991 Jul 29;286(1-2):189-92. doi: 10.1016/0014-5793(91)80971-5.

DOI:10.1016/0014-5793(91)80971-5

PMID:1864368

Abstract

The primary structure of bovine cathepsin S was determined by combining results of protein and peptide sequencing with the sequence deduced from nucleic acid sequencing. Using polymerase chain reaction (PCR) technology, cDNA clones commencing at amino acid 22 of the mature enzyme and continuing through the 3' untranslated region of bovine cathepsin S mRNA were isolated and sequenced. The open reading frame in these overlapping clones correctly predicts the determined amino acid sequence of 13 tryptic peptides derived from purified bovine spleen cathepsin S. The deduced amino acid sequence shows that mature bovine cathepsin S consists of 217 amino acids corresponding to a molecular weight of 23.7 kDa. Cathepsin S belongs to the papain superfamily of lysosomal cysteine proteinases and shares 41% identity with papain. Amino acid sequence identities of bovine cathepsin S to human cathepsins L, H, and B are 56%, 47% and 31% respectively.

摘要

通过将蛋白质和肽测序结果与从核酸测序推导的序列相结合，确定了牛组织蛋白酶S的一级结构。利用聚合酶链反应（PCR）技术，分离并测序了从成熟酶的第22个氨基酸开始并延伸至牛组织蛋白酶S mRNA的3'非翻译区的cDNA克隆。这些重叠克隆中的开放阅读框正确预测了从纯化的牛脾脏组织蛋白酶S衍生的13个胰蛋白酶肽的确定氨基酸序列。推导的氨基酸序列表明，成熟的牛组织蛋白酶S由217个氨基酸组成，分子量为23.7 kDa。组织蛋白酶S属于溶酶体半胱氨酸蛋白酶的木瓜蛋白酶超家族，与木瓜蛋白酶有41%的同源性。牛组织蛋白酶S与人组织蛋白酶L、H和B的氨基酸序列同源性分别为56%、47%和31%。