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  • 1
    Electronic Resource
    Electronic Resource
    Cloning and mapping of the CYS4 gene of Saccharomyces cerevisiae (1992)
    Springer
    Current genetics 21 (1992), S. 285-289 
    Details
    ISSN: 1432-0983
    Keywords: Saccharomyces cerevisiae ; Cysteine biosynthetic ; CYS4 ; Mapping
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary A DNA fragment containing the CYS4 gene of Saccharomyces cerevisiae was isolated from a genomic library. The cloned fragment hybridized to the transverse-alternating-field-electrophoresis band corresponding to chromosomes VII and XV. According to the 2 μm DNA chromosome-loss procedure, the cys2 and cys4 mutations, which are linked together and co-operatively confer cysteine dependence, were assigned to chromosome VII. By further mapping involving tetrad analysis, the cys2-cys4 pair was localized between SUP77 (SUP166) and ade3 on the right arm of chromosome VII.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00351684
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  • 2
    Electronic Resource
    Electronic Resource
    Purification of properties of Saccharomyces cerevisiae cystathionine β-synthase (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 10 (1994), S. 333-339 
    Details
    ISSN: 0749-503X
    Keywords: Cystathionine ; β-synthase ; enzyme purification ; amino acid sequence analysis ; catalytic properties ; Saccharomyces cerevisiae ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Cystathionine β-synthase (β-CTSase), which catalyses cystathionine synthesis from serine and homocysteine, was purified to homogeneity from Saccharomyces cerevisiae. The molecular mass of the enzyme was estimated to be 235 kDa by gel filtration and 55 kDa by sodium dodecyl sulphate-polyacrylamide gel electrophoresis, indicating that it is a homotetramer. The N-terminal amino acid sequence of the enzyme perfectly coincided with that deduced from the nucleotide sequence of CYS4, except for the absence of initiation methionine. The purified β-CTSase catalysed cysteine synthesis from serine (or O-acetylserine) and H2S. From this finding, we discuss the multifunctional nature and evolutionary divergence of S-metabolizing enzymes.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320100306
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