Limited Proteolysis of Silkworm Antitrypsin by Several Proteinases(Biological Chemistry)
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概要
- 論文の詳細を見る
Silkworm antitrypsin (sw-AT) isolated from larval hemolymph was limitedly digested by Achromobacter lysylendopeptidase, α-chymotrypsin, subtilisin BPN', subtilisin Carlsberg, papain, or Pseudomonas elastase. Each proteinase could cleave specific site(s) around the reactive site identified for the reaction of sw-AT and bovine trypsin. Among these proteinases, only subtilisin BPN' was inhibited by sw-AT, although weakly. By the cleavable amino acid sequence in sw-AT, it was suggested that whether or not these proteinases were inhibited by sw-AT did not solely depend on their substrate specificities. The susceptibility to the attack of proteinase should indicate that this region is exposed on the molecular surface. The amino acid sequence in the COOH-terminal region slightly away from the reactive site in sw-AT had homology with that in the corresponding region of the serine proteinase inhibitor (serpin) group.
- 社団法人日本農芸化学会の論文
- 1990-01-23
著者
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TAKAGI Hiroshi
Department of Surgery II, University School of Medicine
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Sasaki Takuji
Department Of Molecular Genetics National Institute Of Agrobiological Sciences
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Takagi H
Murata Manufacturing Co. Ltd. Kyoto Jpn
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Sasaki T
Nagoya Univ. Aichi Jpn
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KOHARA Atuko
Department of Food Science and Technology, School of Agriculture, Nagoya University
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SHIMIDZU Takaaki
Department of Food Science and Technology, School of Agriculture, Nagoya University
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Kohara Atuko
Department Of Food Science And Technology School Of Agriculture Nagoya University
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Shimidzu Takaaki
Department Of Food Science And Technology School Of Agriculture Nagoya University
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Sasaki Takuji
Department Of Food Science And Technology Faculty Of Agriculture Nagoya University
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Takagi Hiroshi
Department Of Bioscience Fukui Prefectural University
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Takagi Hiroshi
Department Of Food Science And Technology School Of Agriculture Nagoya University
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Takagi Hiroshi
Department Of Bioscience Faculty Of Bioscience Fukui Prefectural University
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