Cole T C, Melrose J, Ghosh P
Raymond Purves Research Laboratories, University of Sydney, St. Leonards, Australia.
Biochim Biophys Acta. 1989 Mar 24;990(3):254-62. doi: 10.1016/s0304-4165(89)80042-x.
A neutral proteinase of 94 kDa capable of degrading gelatin, canine disc proteoglycan, and L-lysine and L-arginine peptide substrates has been isolated from the greyhound intervertebral disc. Strong inhibition of this proteinase with class-specific inhibitors, such as APMSF, TLCK and benzamidine indicated a 'serine'-type specificity. Metallo, aspartyl- and cysteine proteinase inhibitors were devoid of significant action. Degradation of the resident canine disc proteoglycan monomer by the disc proteinase was shown to occur at the hyaluronic acid binding region, thereby diminishing its ability to aggregate with hyaluronic acid. The hydrodynamic size of the proteoglycan degradation products was only slightly less than that of the intact disc proteoglycan subunits.
从灵缇犬椎间盘分离出一种94 kDa的中性蛋白酶，它能够降解明胶、犬椎间盘蛋白聚糖以及L - 赖氨酸和L - 精氨酸肽底物。用APMSF、TLCK和苯甲脒等类别特异性抑制剂对该蛋白酶进行的强烈抑制表明其具有“丝氨酸”型特异性。金属蛋白酶、天冬氨酸蛋白酶和半胱氨酸蛋白酶抑制剂均无显著作用。椎间盘蛋白酶对犬椎间盘内源性蛋白聚糖单体的降解发生在透明质酸结合区域，从而降低了其与透明质酸聚集的能力。蛋白聚糖降解产物的流体力学大小仅略小于完整椎间盘蛋白聚糖亚基的大小。
