Major extracellular protease of Neurospora crassa.
The inducible extracellular alkaline protease of Neurospora crassa was demonstrated to be a glycoprotein containing D-galactose residues by use of the enzyme-lectin conjugate horseradish peroxidase-Ricinus communis-agglutinin-120. The carbohydrate moiety of the protease appears to be a poor antigen since an antiserum made to the native enzyme recognizes epitopes determined only by the polypeptide portion of the enzyme. Immunochemical techniques were used to quantitatively precipitate protease labeled in vivo for electrophoretic analysis. Protease synthesis could not be detected in control, uninduced cultures, whereas ca. 0.4% of total cellular protein synthesis is devoted to protease formation under inducing conditions.
D000906:Antibodies; D000936:Antigen-Antibody Complex; D002241:Carbohydrates / Q000032:analysis; D010450:Endopeptidases / Q000096:biosynthesis / Q000302:isolation & purification* / Q000378:metabolism; D004790:Enzyme Induction; D006023:Glycoproteins / Q000302:isolation & purification; D007700:Kinetics; D009491:Neurospora / Q000201:enzymology*; D009492:Neurospora crassa / Q000201:enzymology*; D012697:Serine Endopeptidases
D000906:Antibodies; D000936:Antigen-Antibody Complex; D002241:Carbohydrates; D006023:Glycoproteins; D010450:Endopeptidases; D012697:Serine Endopeptidases; C032923:microbial serine proteinases