Single Site Proteolysis in Silkworm Antitrypsin Causes Structural Changes in Behavior against Denaturing Reagents(Biological Chemistry)
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概要
- 論文の詳細を見る
Silkworm antitrypsin (sw-AT), which was thought to belong to serpin family, changed its behavior against denaturation after chymotryptic cleavage of a single peptide bond (Tyr-Val) two amino acids away from the reactive site for trypsin (Lys-Val). This chymotrypsin-modified sw-AT became resistant to denaturation by heat, sodium dodecyl sulfate, or guanidine hydrochloride, and this characteristic was evident in its circular dichroism spectrum. The modified sw-AT was also indigestible by S. aureus V8 protease. These facts should indicate a structural change from a stressed, unstable state to a stable one accompanying the cleavage of the single peptide bond in sw-AT. The stabilizing factor was in part attributed to the interaction of a COOH-terminal fragment (5kDa) and an NH_2-terminal one (36kDa) in modified sw-AT.
- 社団法人日本農芸化学会の論文
- 1990-01-23
著者
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Kobayashi Kazuto
Department of Research and DevelopmentHonda, Electronics Co., Ltd.
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Sasaki Takuji
Department Of Molecular Genetics National Institute Of Agrobiological Sciences
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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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Kobayashi Kazuto
Department Of Cardiovascular Medicine Okayama University
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Kobayashi Kazuto
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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