Vogel K G, Koob T J, Fisher L W
Department of Biology, University of New Mexico, Albuquerque.
Biochem Biophys Res Commun. 1987 Oct 29;148(2):658-63. doi: 10.1016/0006-291x(87)90927-2.
Sequence analysis showed that Staphylococcus aureus V8 protease cleaved the core protein of the small dermatan sulfate proteoglycan of bovine tendon (PGII) on the carboxy side of a glutamic acid residue located 17 amino acids from the N-terminus of the intact molecule. The remaining 40 kDa core protein fragment inhibited collagen fibrillogenesis in an in vitro assay. V8 protease readily generated this fragment in tendon tissue, but it was not released from the tissue during treatment. These results indicate that neither the 17-amino acid N-terminal peptide nor the glycosaminoglycan chain attached to this peptide is required for maintaining the interaction of this proteoglycan with a collagen matrix.
序列分析表明，金黄色葡萄球菌V8蛋白酶在完整分子N端起第17个氨基酸的谷氨酸残基的羧基侧切割牛腱小硫酸皮肤素蛋白聚糖（PGII）的核心蛋白。在体外试验中，剩余的40 kDa核心蛋白片段抑制了胶原纤维形成。V8蛋白酶能在腱组织中轻易产生该片段，但在处理过程中它并未从组织中释放出来。这些结果表明，对于维持该蛋白聚糖与胶原基质的相互作用而言，17个氨基酸的N端肽及其连接的糖胺聚糖链均非必需。
