ブタ精巣ヒアルロニダーゼの部分精製とその酵素性質

概要

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Hyaluronidase (HAase) [EC 3.2.1.36] was partially purified about 500-fold from pig testis by gel filtration on Sephadex G-100 and ion-exchange chromatographies on CM-52 and DE-52 cellulose. The partially purified HAase hydrolyzed both hyaluronic acid and chondroitin 4-sulfate in the optimal pH range from 5.0 to 5.2,but the enzyme did not have chondro-4- and -6-sulfatase activities. For the maximal hydrolysis of hyaluronic acid, the enzyme required the presence of NaCl in the reaction system, whereas high concentration of the salt inhibited significantly the enzyme. Although partially purified HAase was eluted in a single peak corresponding to mol. wt of 61 K from the column of Sephadex G-100,the enzyme was separated into several moieties with different isoelectric points (about 8,6.9,6.7,6.5 and less than 6.5) by the chromatofocusing, indicating the presence of isoenzymes of HAase.
公益社団法人日本薬学会の論文
1985-01-25