Perides G, Asher R A, Lark M W, Lane W S, Robinson R A, Bignami A
Harvard Medical School, Department of Pathology, Boston, MA 02132, USA.
Biochem J. 1995 Dec 1;312 ( Pt 2)(Pt 2):377-84. doi: 10.1042/bj3120377.
Glial hyaluronate-binding protein (GHAP) is a 60 kDa glycoprotein with an amino acid sequence identical to that of the hyaluronate-binding region of versican, a large fibroblast aggregating proteoglycan found in the brain. Both GHAP and versican were identified by immunoblot in bovine brain extracts prepared only minutes after death. Human recombinant collagenase, stromelysin, mouse gelatinase and gelatinases isolated from human brain by affinity chromatography digest versican and give rise to a polypeptide with electrophoretic mobility identical to GHAP. Immunoblot analysis, peptide mapping and C-terminal amino acid sequencing indicate that the polypeptide generated by digestion with human brain gelatinases is identical to GHAP. We suggest that GHAP is a naturally occurring versican degradation product.
神经胶质透明质酸结合蛋白（GHAP）是一种60 kDa的糖蛋白，其氨基酸序列与多功能蛋白聚糖的透明质酸结合区域相同，多功能蛋白聚糖是一种在大脑中发现的大型成纤维细胞聚集蛋白聚糖。在牛死后仅几分钟制备的脑提取物中，通过免疫印迹法鉴定出了GHAP和多功能蛋白聚糖。人重组胶原酶、基质溶素、小鼠明胶酶以及通过亲和层析从人脑中分离出的明胶酶均可消化多功能蛋白聚糖，并产生一种电泳迁移率与GHAP相同的多肽。免疫印迹分析、肽图分析和C端氨基酸测序表明，人脑明胶酶消化产生的多肽与GHAP相同。我们认为GHAP是一种天然存在的多功能蛋白聚糖降解产物。
