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A heat-labile serine proteinase from Penicillium citrinum
N Yamamoto1, K Matsumoto, Y Yamagata
1Department of Applied Biological Chemistry, Faculty of Agriculture, Tohoku University, Sendai, Japan.
Phytochemistry
|April 1, 1993
Abstract:
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.