Purification of a serine-proteinase inhibitor from human articular cartilage. Identity with the acid-stable proteinase inhibitor of mucous secretions.
Purification of a serine-proteinase inhibitor from human articular cartilage. Identity with the acid-stable proteinase inhibitor of mucous secretions.
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从人关节软骨中纯化丝氨酸蛋白酶抑制剂。
作者：
Beate Bohm;Rainer DEUTZMANNt;H. Burkhardt
从人关节软骨中纯化出了丝氨酸蛋白酶人白细胞弹性蛋白酶（EC 3.4.21.37）、组织蛋白酶G （EC 3.4.21.20）和胰蛋白酶（EC 3.4.21.4）的抑制剂。用SDS/PAGE测定阳离子蛋白（pI大于10）的表观Mr为15000。Western blot结果显示，该蛋白与重组蛋白衍生的人粘膜分泌物丝氨酸蛋白酶抑制剂的特异性抗体发生交叉反应。通过测定软骨来源的丝氨酸蛋白酶抑制剂的n端氨基酸序列，可以确定这两种抑制剂的身份。在所有24个残基中，软骨抑制剂被证明与人分泌性白细胞蛋白酶抑制剂（SLPI）相同。抑制分子可能在保护软骨基质蛋白免受蛋白水解攻击中起关键作用。
An inhibitor of the serine proteinases human leucocyte elastase (EC 3.4.21.37), of cathepsin G (EC 3.4.21.20) and of trypsin (EC 3.4.21.4) has been purified from human articular cartilage. The apparent Mr of the cationic (pI greater than 10) protein was determined to 15,000 by SDS/PAGE. It was shown to cross-react in Western blot with a specific antibody to a recombinant-derived serine-proteinase inhibitor of human mucous secretions. Identity of both inhibitors is indicated by the determination of the N-terminal amino acid sequence of the cartilage-derived serine-proteinase inhibitor. In all 24 residues the cartilage inhibitor was shown to be identical with the human secretory leucocyte proteinase inhibitor ('SLPI'). The inhibitor molecule may play a crucial role in the protection of cartilage matrix proteins against proteolytic attack.