A serine proteinase from Penicillium citrinum was purified. The M(r) a
nd isoelectric point were determined as about 26 000 and 9.5, respecti
vely. 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 am
ino acids in the N-terminal region were ANVVQSNVPSWGLARISSK-RPGTTSYTYD
STAGEGVVFYGVDTG. The specificity differs from that of other serine pro
teinases. Kinetic studies on fluorogenic substrates were determined.