Purification and characterization of an aminopeptidase from the fungusSaccobolus platensis
A major aminopeptidase was purified to apparent homogeneity from soluble extracts of the fungusSaccobolus platensis by DEAE-cellulose, phenyl-Sepharose, Sephacryl S-300 chromatography, and disc polyacrylamide gel electrophoresis. Peptidase activity was measured with the radioactive peptide substrate...
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| Autores principales: | , , |
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| Formato: | JOUR |
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| Acceso en línea: | http://hdl.handle.net/20.500.12110/paper_01475975_v16_n4_p279_Murray |
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| Sumario: | A major aminopeptidase was purified to apparent homogeneity from soluble extracts of the fungusSaccobolus platensis by DEAE-cellulose, phenyl-Sepharose, Sephacryl S-300 chromatography, and disc polyacrylamide gel electrophoresis. Peptidase activity was measured with the radioactive peptide substrate Leu-Arg-Arg-Ala-Ser[32P]-Leu-Gly. The purified enzyme was a monomeric protein with a molecular mass of 90 kDa. The optimun pH of the enzyme activity was in the range 7.4-7.6. It was inhibited remarkably by EDTA, 1,10-phenanthroline, puromycin, amastatin, bestatin, and hydrophobic amino acids. The enzyme had a low substrate specificity and a requirement for free α-amino groups. Saccobolus peptidase had no measurable endoproteolytic activity and the exoproteolytic activity was evidenced on small peptides, suggesting that it might be involved in the late stage of protein turnover events. © 1992 Academic Press, Inc. |
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