A heat-labile serine proteinase from Penicillium citrinum.
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.
Yamamoto
N
N
Department of Applied Biological Chemistry, Faculty of Agriculture, Tohoku University, Sendai, Japan.
Matsumoto
K
K
Yamagata
Y
Y
Hirano
K
K
Ichishima
E
E
D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D007328:Insulin / Q000378:metabolism; D008969:Molecular Sequence Data; D010407:Penicillium / Q000201:enzymology*; D012697:Serine Endopeptidases / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D013379:Substrate Specificity
D007328:Insulin; D012697:Serine Endopeptidases