Isolation and Characterization of a Possible Native Cucumisin from Developing Melon Fruits and Its Limited Autolysis to Cucumisin(Biological Chemistry)
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概要
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A serine proteinase was purified to an electrophoretically homogeneous state from developing fruits of Prince melon (Cucumis melo L. var. Prince). Its molecular mass was 67 kD by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, which was apparently different from that of cucumisin (50 kD), a serine proteinase previously isolated from Prince melon. When the purified 67-kD enzyme was incubated at 50℃ and pH 7.2, it was split into a 54-kD proteinase and a 14-kD polypeptide by limited autolysis without any loss of the caseinolytic activity. Commercial cucumisin preparation was found to contain the 67- and 54-kD proteinases. The content of each amino acid residue in the 67-kD enzyme was higher than that in the 54-kD proteinase or cucumisin. Thus, it was concluded that the purified 67-kD enzyme is a native form of cucumisin, and that cucumisin is a product derived by the limited autolysis of the 67-kD proteinase. The 67-kD proteinase was more stable than the 54-kD one at acidic pHs.
- 1989-04-23
著者
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Yamagata Hiroshi
Laboratory Of Biochemistry Faculty Of Agriculture Kobe University
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Iwasaki Teruo
Laboratory Of Biochemistly Faculty Of Agriculture Kobe University
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UENO Shuji
Laboratory of Biochemistry, Faculty of Agriculture, Kobe University
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Ueno Shuji
Laboratory Of Biochemistry Faculty Of Agriculture Kobe University
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