Partial purification of the enzyme obtained from the rat kidney microsomal membrane with succinyl trialanine p-nitroanilide-hydrolyzing activity and the one similar to signal peptidase.
抄録
An endopeptidase was obtained from the rat kidney microsomal membrane through its treatment with 1M-KCl, Brij 35 and Nonidet P-40, and subsequently by DEAE-Sephadex chromatography and Sepharose CL-6B gel filtration, in which process the enzyme was subjected to partial purification by means of the substrate succinyl trialanine p-nitroanilide. We found the enzyme cleaves the substrate into succinyl dialanine and alanine p-nitroanilide. Further, the posttranslational processing experiments have revealed the presence of an activity in the partially purified enzyme to cleave the prehuman placental lactogen (pre-hPL) into its mature form (hPL).
収録刊行物
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- ＣＨＥＭＩＣＡＬ ＆ ＰＨＡＲＭＡＣＥＵＴＩＣＡＬ ＢＵＬＬＥＴＩＮ
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ＣＨＥＭＩＣＡＬ ＆ ＰＨＡＲＭＡＣＥＵＴＩＣＡＬ ＢＵＬＬＥＴＩＮ 31 (8), 2940-2943, 1983
公益社団法人 日本薬学会