A heat-labile serine proteinase from Penicillium citrinum.

作者信息

Yamamoto N, Matsumoto K, Yamagata Y, Hirano K, Ichishima E

机构信息

Department of Applied Biological Chemistry, Faculty of Agriculture, Tohoku University, Sendai, Japan.

出版信息

Phytochemistry. 1993 Apr;32(6):1393-7. doi: 10.1016/0031-9422(93)85144-g.

A serine proteinase from Penicillium citrinum was purified. The M(r) and isoelectric point were determined as about 26,000 and 9.5, respectively. Activity was retained up to above 40 degrees at pH 7 for 30 min, but the enzyme was completely inactivated at 50 degrees. The first amino acids in the N-terminal region were ANVVQSNVPSWGLARISSKRPGTTSYTYDSTAGEGVVFYGVDTG. The specificity differs from that of other serine proteinases. Kinetic studies on fluorogenic substrates were determined.