TY - JOUR
T1 - Purification of 35K protease from the digestive juice of Bombyx mori
AU - Jiang, Yonghuang
AU - Shirai, Koji
AU - Okido, Toshihisa
AU - Banno, Yutaka
AU - Fujii, Hiroshi
PY - 2000
Y1 - 2000
N2 - 35K protease was purified from the digestive juice of Bombyx mori by a series of chromatography using Butyl-Toyopearl, Sephadex G-50 and DEAE-Sephacel. The purified protease gave a single protein band with a molecular mass of 35,000 on SDS-PAGE and its pi was 9. 1. It had optimal activity at pH11 and in the temperature under 40°C. The enzyme activity was almost completely lost at 60°C and at pH4. It was slightly inhibited by Cu2+and Mn2+, and strongly by diisopropylfluorophosphate, phenylmethylsulfonylfluoride and chymostatin, suggesting that the enzyme may be a chymotrypsin-like protease.
AB - 35K protease was purified from the digestive juice of Bombyx mori by a series of chromatography using Butyl-Toyopearl, Sephadex G-50 and DEAE-Sephacel. The purified protease gave a single protein band with a molecular mass of 35,000 on SDS-PAGE and its pi was 9. 1. It had optimal activity at pH11 and in the temperature under 40°C. The enzyme activity was almost completely lost at 60°C and at pH4. It was slightly inhibited by Cu2+and Mn2+, and strongly by diisopropylfluorophosphate, phenylmethylsulfonylfluoride and chymostatin, suggesting that the enzyme may be a chymotrypsin-like protease.
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U2 - 10.11416/kontyushigen1930.69.47
DO - 10.11416/kontyushigen1930.69.47
M3 - Article
AN - SCOPUS:33746384772
SN - 0037-2455
VL - 69
SP - 47
EP - 53
JO - Journal of Sericultural Science of Japan
JF - Journal of Sericultural Science of Japan
IS - 1
ER -