Purification of an acid protease from Mucor rouxii that inactivates chitin synthetase |
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Authors: | S Diaz J Ruizherrera |
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Affiliation: | (1) Departmento de Genética y Biología Molecular, Centro de Investigación y Estudios Avanzados, I.P.N., Mexico;(2) Instituto de Investigación en Biología Experimental, Facultad de Química, Universidad de Guanajuato, Apartado Postal 187, 36000 Guanajuato, Gto, Mexico |
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Abstract: | An acid protease was purified from the mycelial form of Mucor rouxii by a method which involved salt and acid precipitation, gel filtration and anion-exchange chromatography. The enzyme had a molecular mass of 16,000 Da. Its optimum pH was 4.0, maximal activity was obtained at 50°C, and it was inactivated at 70°C. It was not affected by leupeptin or N -p-tosyl-L-lysine chloromethyl ketone (TLCK) but diazoacetyl-DL-norleucine methyl ester (DNME) in the presence of Cu2+ and more noticeably pepstatin A, strongly inhibited the activity. This acid protease did not activate zymogenic chitin synthetase from the fungus, but brought about its inactivation even at low concentrations and after short periods of incubation time.Abbreviations TLCK
N -p-tosyl-L-lysine chloromethyl ketone
- DNME
diazoacetyl-DL-norleucine methyl ester
- TCA
trichloroacetic acid
- SDS
sodium dodecyl sulfate |
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Keywords: | acid protease chitin synthetase Mucor |
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