Purification and characterization of cysteine protease from Pleurotus ostreatus.
Cysteine protease activity in mycelial culture increased 7.7-fold after fruit body formation in Pleurotus ostreatus, using the Leu pNA (LPNA) cleavage assay. The enzyme was purified from fruit bodies and its M(r) was 97,000 by gel filtration and 48,500 by SDS-PAGE, indicating that it is a dimer. The enzyme was sensitive to iodoacetic acid, p-chloromercuribenzoate, N-ethylmaleimide, and HgCl2. The sequence of the first 9 N-terminal amino acids of cysteine protease was ASGLXXAIL.
Department of Microbiology, University of Ulsan, Korea.
H H
HH
Shin
H S
HS
Choi
D001487:Basidiomycota / Q000201:enzymology*; D002729:Chloromercuribenzoates / Q000737:chemistry; D002850:Chromatography, Gel; D003546:Cysteine Endopeptidases / Q000737:chemistry / Q000302:isolation & purification*; D019281:Dimerization; D004591:Electrophoresis, Polyacrylamide Gel; D005033:Ethylmaleimide / Q000737:chemistry; D006863:Hydrogen-Ion Concentration; D007461:Iodoacetates / Q000737:chemistry; D019807:Iodoacetic Acid; D008627:Mercuric Chloride / Q000737:chemistry; D008970:Molecular Weight
D002729:Chloromercuribenzoates; D007461:Iodoacetates; D008627:Mercuric Chloride; D003546:Cysteine Endopeptidases; D005033:Ethylmaleimide; D019807:Iodoacetic Acid