Functional Expression and Enzymatic Properties of Two Sitophilus zeamais Cysteine Proteinases Showing Different Autolytic Processing Profiles In Vitro.
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概要
- 論文の詳細を見る
To characterize in more detail the cathepsin L-like cysteine proteinases from Sitophilus zeamais (SCPs) cloned in our previous study [Matsumoto et al. (1997) J. Biochem. 121, 464-476], we established a system for their functional expression and purification using a glutathione S-transferase (GST) fusion gene vector from Escherichia coli. The proenzyme forms of two representative SCPs, proSCPc1 and proSCPg3, were expressed as GST-fusion proteins and purified on a glutathione Sepharose column. GST-proSCPc1 undergoes autoproteolytic cleavage into the mature form efficiently at acidic pH, and exhibits significant proteolytic activity toward various substrates including hemoglobin and Z-Phe-Arg-MCA. The enzymatic characteristics of the activated form of SCPc1 are similar to those of mammalian cathepsin L, but its pH optimum for the hydrolysis of hemoglobin is significantly lower. The other proSCP, GST-proSCPg3, which has a shorter COOH-terminal domain than SCPc1, undergoes almost no autolytic processing and shows only very slight proteolytic activity, although the other enzymatic characteristics of GST-proSCPg3 are similar to those of GST-proSCPc1.
- 社団法人 日本生化学会の論文
著者
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Emori Yasufumi
Department Of Applied Biological Chemistry Graduate School Of Agricultural And Life Sciences The Uni
-
Abe Keiko
Department Of Agricultural Chemistry The University Of Tokyo
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Matsumoto Ichiro
Department Of Applied Biological Chemistry Graduate School Of Agricultural And Life Sciences The Uni
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ARAI Soichi
Department of Agricultural Chemicatry, The University of Tokyo
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Emori Yasufumi
Department of Biophysics and Biochemistry, Faculty of Science, The University of Tokyo
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