来自牛牙龈的两种伴刀豆球蛋白A未结合型胶原酶抑制剂的部分测序

Partial sequencing of two forms of concanavalin A-unbound collagenase inhibitor from bovine gingiva.

作者信息

Mizuno T, Igarashi A, Nohara H

机构信息

Department of Biochemistry, Niigata University School of Dentistry, Japan.

出版信息

Arch Oral Biol. 1993 Oct;38(10):917-8. doi: 10.1016/0003-9969(93)90102-r.

DOI:10.1016/0003-9969(93)90102-r

PMID:8279996

Abstract

Three forms of collagenase inhibitor, one ConA-bound and two ConA-unbound, were extensively purified from bovine gingiva by sequential column chromatography. Analysis by sodium dodecyl sulphate-polyacrylamide gel electrophoresis revealed that inhibitory activity resides in proteins with M(r) of 26000-28000 and 22000 for ConA-bound and two ConA-unbound inhibitors, respectively. Of these, two ConA-unbound inhibitors were partially sequenced in the first 12 amino acids and found to have an identical sequence. The NH2-terminal sequence had 100% identity with TIMP-2 or MI.

摘要

通过连续柱色谱法从牛牙龈中广泛纯化出三种形式的胶原酶抑制剂，一种与刀豆球蛋白A（ConA）结合，两种未与ConA结合。十二烷基硫酸钠-聚丙烯酰胺凝胶电泳分析表明，与ConA结合的抑制剂和两种未与ConA结合的抑制剂的抑制活性分别存在于分子量为26000 - 28000和22000的蛋白质中。其中，对两种未与ConA结合的抑制剂的前12个氨基酸进行了部分测序，发现它们具有相同的序列。其氨基末端序列与金属蛋白酶组织抑制因子-2（TIMP-2）或MI具有100%的同一性。