NEUROSPORA TYROSINASE

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منابع مشابه

Isolation and characterization of the tyrosinase gene from Neurospora crassa.

A precursor form of Neurospora crassa tyrosinase has been identified by Western transfer from crude protein extracts and by immunoprecipitation of in vitro translated tyrosinase mRNA. The molecular weight of protyrosinase (75,000) exceeds that of mature tyrosinase (46,000) by about 50%. In order to deduce the primary structure and the nature of the extension, the tyrosinase gene was cloned. Pol...

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Amino acid sequence of tyrosinase from Neurospora crassa.

The amino-acid sequence of tyrosinase from Neurospora crassa (monophenol,dihydroxyphenylalanine:oxygen oxidoreductase, EC 1.14.18.1) is reported. This copper-containing oxidase consists of a single polypeptide chain of 407 amino acids. The primary structure was determined by automated and manual sequence analysis on fragments produced by cleavage with cyanogen bromide and on peptides obtained b...

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A comparison of the properties of two forms of tyrosinase from Neurospora crassa.

The differences between a thermostable (T”) and thermolabile ( TL) form of tyrosmase from Neurospora crassa have been studied by means of a spectrophotometric technique using ascorbate or ferrocyanide. No significant differences in substrate specificit> have been found in a survey of over 30 substances which included mono-, di-, tri-, and conjugated phenols. Catechol was found to be a substrate...

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Derepression of tyrosinase synthesis in Neurospora by cycloheximide, actinomycin D, and puromycin.

Cycloheximide, actinomycin D, and puromycin inhibit the synthesis de novo of tyrosinase in cultures of Neurospora crassa which have been derepressed by fasting. Under other conditions, or in a mutant which is not derepressed by fasting, these antibiotics derepress the synthesis at low concentrations. Derepressed cultures, after a lag period, produce tyrosinase at an initially exponential rate. ...

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A genetic study of two new structural forms of tyrosinase in Neurospora.

N previous work from this laboratory, three apparently unlinked genes conIcerned with the synthesis of tyrosinase in Neurospora crassa have been identified. These genes, designated T , ty-1, and ty-2, respectively, are not functionally equivalent. It was found that whereas the T locus has a structure-determining role in the synthesis of the enzyme, the genes ty-1 and ty-2 determine whether tyro...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1952

ISSN: 0021-9258

DOI: 10.1016/s0021-9258(18)55606-4