Hydrolytic profile for ester-or amide-linkage by carboxylesterases pI 5.3 and 4.5 from human liver.

…, T SUGIYAMA, Y KATAGIRI, M TATEMATSU…

文献索引：Takai, Satomi; Matsuda, Ayuka; Usami, Yoshiko; Adachi, Tetsuo; Sugiyama, Tadashi; Katagiri, Yoshihiro; Tatematsu, Masae; Hirano, Kazuyuki Biological and Pharmaceutical Bulletin, 1997 , vol. 20, # 8 p. 869 - 873

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被引用次数: 120

摘要

Carboxylesterases (EC 3.1. 1.1) from human liver were purified using Q-Sepharose, Sephadex G-150, isoelectrofocusing and Con A-Sepharose. The calculated molecular mass of the pI 5.3 enzyme was 120 kDa and 61 kDa from the results of Sephadex G-150 gel filtration and SDS-polyacrylamide gel electrophoresis (PAGE), respectively, suggesting that this enzyme is a dimer. On the other hand, carboxylesterase pI 4.5, with a molecular mass ...