GENETIC DETERMINATION OF TYROSINASE THERMOSTABILITY IN NEUROSPORA

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Genetic Determination of Tyrosinase Thermostability

(HOROWITZ and SHEN 1952). The strain produces almost no tyrosinase activity when cultured at 35" C on a medium which favors the production of strong activity in 25" cultures. The evidence indicated that the temperature effect is not due to formation of a tyrosinase inhibitor, but to a net decrease in tyrosinase synthesis at the higher temperature. Attention has been called to the resemblance be...

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Comparison of amino acid sequence and thermostability of tyrosinase from three wild type strains of Neurospora crassa.

The thermostability of tyrosinase from three wild type strains of Neurospora crassa has been investigated. For this purpose a sequence comparison of two thermostable and one thermolabile tyrosinase isoenzyme was carried out. It revealed that at position 201 the thermostable enzyme forms share an aspartate residue in contrast to an asparagine residue in the thermolabile form. In addition, one of...

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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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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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ژورنال

عنوان ژورنال: Genetics

سال: 1953

ISSN: 1943-2631

DOI: 10.1093/genetics/38.4.360