PubMed:1368516 JSONTXT

{"project":"silkwormbase","denotations":[{"id":"T1","span":{"begin":27,"end":35},"obj":"Species:7091"},{"id":"T2","span":{"begin":115,"end":123},"obj":"Species:7091"},{"id":"T3","span":{"begin":287,"end":294},"obj":"Chemical:-"},{"id":"T4","span":{"begin":353,"end":360},"obj":"Chemical:MESH:C110469"},{"id":"T5","span":{"begin":438,"end":460},"obj":"Chemical:MESH:D012967"},{"id":"T6","span":{"begin":465,"end":488},"obj":"Chemical:MESH:D019791"},{"id":"T7","span":{"begin":575,"end":580},"obj":"Chemical:-"},{"id":"T8","span":{"begin":606,"end":615},"obj":"Species:1280"}],"text":"Single site proteolysis in silkworm antitrypsin causes structural changes in behavior against denaturing reagents.\nSilkworm 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 (5 kDa) and an NH2-terminal one (36 kDa) in modified sw-AT."}

{"project":"silkworm","denotations":[{"id":"T1","span":{"begin":27,"end":35},"obj":"Species:7091"},{"id":"T2","span":{"begin":115,"end":123},"obj":"Species:7091"},{"id":"T3","span":{"begin":287,"end":294},"obj":"Chemical:-"},{"id":"T4","span":{"begin":353,"end":360},"obj":"Chemical:MESH:C110469"},{"id":"T5","span":{"begin":438,"end":460},"obj":"Chemical:MESH:D012967"},{"id":"T6","span":{"begin":465,"end":488},"obj":"Chemical:MESH:D019791"},{"id":"T7","span":{"begin":575,"end":580},"obj":"Chemical:-"},{"id":"T8","span":{"begin":606,"end":615},"obj":"Species:1280"}],"text":"Single site proteolysis in silkworm antitrypsin causes structural changes in behavior against denaturing reagents.\nSilkworm 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 (5 kDa) and an NH2-terminal one (36 kDa) in modified sw-AT."}