牛睫状体和虹膜中组织蛋白酶B的部分纯化
Partial purification of cathepsin B in the bovine ciliary body and iris.
作者信息
Hayasaka S, Shiono T, Hara S, Fukuyo T
出版信息
Invest Ophthalmol Vis Sci. 1983 Jun;24(6):682-6.
Cathepsin B in the bovine ciliary body and iris was studied biochemically using alpha-N-benzoyl-D,L-arginine-2-naphthylamide as substrate. The enzyme was purified to 210-fold from the autolyzed extract. The partially purified enzyme had a pH optimum at 6.0 and a molecular weight of 27,000. The apparent Km value for the substrate was 1.6 mM. The enzyme was activated by disodium ethylenediamine tetraacetate, cysteine, and dithiothreitol. The enzyme activity was inhibited strongly by leupeptin and partially by hyaluronate and chondroitin sulfate A.
以α-N-苯甲酰-D,L-精氨酸-2-萘酰胺为底物，对牛睫状体和虹膜中的组织蛋白酶B进行了生化研究。该酶从自溶提取物中纯化至210倍。部分纯化的酶在pH 6.0时具有最佳活性，分子量为27000。底物的表观Km值为1.6 mM。该酶被乙二胺四乙酸二钠、半胱氨酸和二硫苏糖醇激活。该酶活性受到亮肽素的强烈抑制，并受到透明质酸和硫酸软骨素A的部分抑制。
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