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  • 1
    Electronic Resource
    Electronic Resource
    Subcellular localization of long-chain alcohol dehydrogenase and aldehyde dehydrogenase in n-alkane-grown Candida tropicalis (1980)
    Springer
    Archives of microbiology 128 (1980), S. 145-151 
    Details
    ISSN: 1432-072X
    Keywords: Candida tropicalis ; alkane utilization ; Yeast peroxisomes ; Long-chain alcohol dehydrogenase ; Long-chain aldehyde dehydrogenase ; Acyl-CoA synthetase ; Glycerol-3-phosphate acyltransferase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Long-chain alcohol dehydrogenase and longchain aldehyde dehydrogenase were induced in the cells of Candida tropicalis grown on n-alkanes. Subcellular localization of these dehydrogenases, together with that of acyl-CoA synthetase and glycerol-3-phosphate acyltransferase, was studied in terms of the metabolism of fatty acids derived from n-alkane substrates. Both longchain alcohol and aldehyde dehydrogenases distributed in the fractions of microsomes, mitochondria and peroxisomes obtained from the alkane-grown cells of C. tropicalis. Acyl-CoA synthetase was also located in these three fractions. Glycerol-3-phosphate acyltransferase was found in microsomes and mitochondria, in contrast to fatty acid β-oxidation system localized exclusively in peroxisomes. Similar results of the enzyme localization were also obtained with C. lipolytica grown on n-alkanes. These results suggest strongly that microsomal and mitochondrial dehydrogenases provide long-chain fatty acids to be utilized for lipid synthesis, whereas those in peroxisomes supply fatty acids to be degraded via β-oxidation to yield energy and cell constituents.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00406151
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Purification of peroxisomal malate synthase from alkane-grown Candida tropicalis and some properties of the purified enzyme (1986)
    Springer
    Archives of microbiology 144 (1986), S. 137-141 
    Details
    ISSN: 1432-072X
    Keywords: Malate synthase ; Peroxisomes ; Alkane-grown yeast ; Candida tropicalis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Malate synthase, one of the key enzymes in the glyoxylate cycle, was purified from peroxisomes of alkane-grown yeast, Candida tropicalis. The enzyme was mainly localized in the matrix of peroxisomes, judging from subcellular fractionation followed by exposure of the organelles to hypotonic conditions. The molecular mass of this peroxisomal malate synthase was determined to be 250,000 daltons by gel filtration on a Sepharose 6B column as well as by ultracentrifugation. On sodium dodecylsulfate/polyacrylamide slab-gel electrophoresis, the molecular mass of the subunit of the enzyme was demonstrated to be 61,000 daltons. These results revealed that the native form of this enzyme was homo-tetrameric. Peroxisomal malate synthase showed the optimal activity pH at 8.0 and absolutely required Mg2+ for enzymatic activity. The K m values for Mg2+, acetyl-CoA and glyoxylate were 4.7 mM, 80 μM and 1.0 mM, respectively.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00414723
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    Paper (German National Licenses)
    Fulltext
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