Major extracellular protease of Neurospora crassa.
AUTOR(ES)
Abbott, R J
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=215673Documentos Relacionados
- Extracellular acid proteases from Neurospora crassa.
- Cellulase of Neurospora crassa.
- Relationship between two major immunoreactive forms of arginase in Neurospora crassa.
- Participation of an extracellular deaminase in amino acid utilization by Neurospora crassa.
- Characterization of nit-2, the major nitrogen regulatory gene of Neurospora crassa.
