PURIFICATION AND PROPERTIES OF A PROTEOLYTIC ENZYME, RABBIT CATHEPSIN E, AND FURTHER STUDIES ON RABBIT CATHEPSIN D
PURIFICATION AND PROPERTIES OF A PROTEOLYTIC ENZYME, RABBIT CATHEPSIN E, AND FURTHER STUDIES ON RABBIT CATHEPSIN D
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DOI：
10.1042/bj0840455
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发表时间：
1962-01-01
影响因子：
4.1
通讯作者：
WEBB, T
中科院分区：
文献类型：
--
作者：
LAPRESLE, C;WEBB, T
两种蛋白水解酶被发现在相对大量的兔骨髓水提取物。这些酶中有一种与Lapresle和Webb（1960）从兔脾中获得的酶相同，被命名为兔组织蛋白酶D。描述了纯化组织蛋白酶D的进一步步骤。其在pH 8.2的琼脂凝胶中的电泳迁移率为~ 17 × 10- 5cm。2 v-1秒- 1.另一种蛋白水解酶被命名为兔组织蛋白酶E。它已被纯化，通过色谱上的二乙基氨基乙基纤维素和凝胶过滤与Sephadex G-75。在家兔脾脏中仅少量存在。以人血清白蛋白为底物，组织蛋白酶E的最适pH为2.5，并且不受半胱氨酸、碘乙酸盐或二异丙基氟磷酸盐的影响。它是热不稳定的。组织蛋白酶E不水解组织蛋白酶A、B和C的合成底物。组织蛋白酶E在pH 8.2的琼脂凝胶中的电泳迁移率为~ 7.2 X 10-5 cm 2。v-1秒- 1.
Two proteolytic enzymes were found in relatively large amounts in aqueous extracts of rabbit bone marrow. One of these enzymes was shown to be the same as the enzyme obtained from rabbit spleen by Lapresle and Webb (1960), and has been named rabbit cathepsin D. A further step in the purification of cathepsin D is described. Its electrophoretic mobility in agar gel at pH 8.2 was -17 x 10-5 cm. 2v-1 sec.-1. The other proteolytic enzyme has been named rabbit cathepsin E. It has been purified by chromatography on diethylaminoethylcellulose and gel-filtration with Sephadex G-75. It is present in only small amounts in rabbit spleen. With human serum albumin as substrate, cathepsin E has an optimum pH at 2.5, and is not affected by cysteine, iodoacetate or di-isopropyl phosphorofluoridate. It is heat-labile. Cathepsin E does not hydrolyse the synthetic substrates for cathepsins A, B and C. The electrophoretic mobility of cathepsin E in agar gel at pH 8.2 is -7.2 X 10-5 cm2. v-1 sec.-1.