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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Biochemical genetics 22 (1984), S. 153-168 
    ISSN: 1573-4927
    Keywords: alcohol dehydrogenase ; Drosophila ; activity ratio ; specific activity
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Thirteen Drosophila Adh variants have been characterized with respect to gene expression, substrate preference, thermostability, and specific activity. The results suggest that the variants may be grouped into two biochemical classes, typified by the properties of the two most common enzyme forms, ADH-F and ADH-S. Membership of these classes cannot be predicted from electrophoretic mobility, nor is any simple classification possible with regard to the characteristics of level of gene expression (in terms of ADH activity or ADH protein) or thermostability of the gene product.
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  • 2
    ISSN: 1573-4927
    Keywords: Drosophila ; glycerol-3-phosphate dehydrogenase ; restriction map ; duplication ; enzyme activity
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Restriction site variation in a 25-kb region including thesn-glycerol-3-phosphate dehydrogenase (Gpdh) locus has been assessed in 29 single femaleD. melanogaster lines from the Cardwell (Australia, QLD) population. TheGpdh locus was duplicated in about one-third of the lines, although the duplication was incomplete and lacked exons 1 and 2. There was no restriction site variation in the duplicated region. Three insertions were found in the gene region but only one affected GPDH activity. The lines with the duplication had higher levels of GPDH activity and protein amount than did nonduplicated lines. This effect was also observed in lines extracted from two other Australian populations. The duplication is shown to have a similar structure in each population investigated and is also present in populations from China and Africa. It is suggested that the effect of the duplication on GPDH activity, which might be due to structural factors affecting transcription at theGpdh locus, could account for the worldwide distribution of the duplication.
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  • 3
    ISSN: 1573-4927
    Keywords: Drosophila ; glycerol-3-phosphate ; dehydrogenase ; low activity ; DNA sequence
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Northern analyses of two low-activitysn-glycerol-3-phosphate dehydrogenase(Gpdh) alleles extracted from natural populations ofDrosophila melanogaster showed that one of them,Gpdh ACyg22 , produced wild-type levels of a normal sized (1.7-kb) mRNA but the other,Gpdh AMB5 , had very low levels of a 1.7-kb mRNA together with low levels of a transcript 200 bp larger. The two variant genes were cloned and sequenced. Compared with normal activity alleles, there were two nucleotide differences in the DNA sequence ofGpdh ACyg22 which were in first-codon positions and would be expected to give rise to Asn-13 → Tyr and Arg-272 → Cys substitutions. The second of these changes is most likely to account for the altered properties of the enzyme. In contrast, none of the nucleotide differences inGpdh AMB5 would give rise to amino acid substitutions, but a 76-bp deletion in the 5′ region removed the normal TATA box and there was a 20-bp insertion in the same region. One of the two transcripts was derived from the use of a substitute TATA box sequence in the insertion, but the 1.9-kb transcript had heterogeneous 5′ ends that were not associated with substitute TATA box sequences. The two transcripts either are produced at a lower rate or are less stable than the normal mRNA.
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  • 4
    ISSN: 1573-4927
    Keywords: Drosophila ; glycerol-3-phosphate dehydrogenase ; restriction map ; duplication ; enzyme activity
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Restriction site variation in a 25-kb region including thesn-glycerol-3-phosphate dehydrogenase (Gpdh) locus has been assessed in 29 single femaleD. melanogaster lines from the Cardwell (Australia, QLD) population. TheGpdh locus was duplicated in about one-third of the lines, although the duplication was incomplete and lacked exons 1 and 2. There was no restriction site variation in the duplicated region. Three insertions were found in the gene region but only one affected GPDH activity. The lines with the duplication had higher levels of GPDH activity and protein amount than did nonduplicated lines. This effect was also observed in lines extracted from two other Australian populations. The duplication is shown to have a similar structure in each population investigated and is also present in populations from China and Africa. It is suggested that the effect of the duplication on GPDH activity, which might be due to structural factors affecting transcription at theGpdh locus, could account for the worldwide distribution of the duplication.
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  • 5
    ISSN: 1573-6857
    Keywords: Gpdh ; allozyme ; Drosophila ; DNA sequence
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Six naturally occurring but rare alleles of sn-glycerol-3-phosphate dehydrogenase (Gpdh) in Drosophila melanogaster have been investigated in this study. They all belong to a class of Gpdh UF (ultra-fast) alleles, because their electrophoretic mobilities are faster than that of the Gpdh F (fast) allele. The Gpdh UF variants are widespread, and have been reported from five continents. DNA sequence analysis has shown that the change in electrophoretic mobility was in each allele caused by a single amino acid residue substitution in the encoded protein. In the Xiamen UF allele it is a substitution of lysine (AAA) to asparagine (AAT) in exon 1 (residue 3). An asparagine (AAT) to aspartate (GAT) change was found in exon 6 (residue 336) in the Iowa UF and Netherlands UF alleles. The mobility of the Raleigh UF allele was altered by a valine (GTG) to glutamate (GAG) substitution in exon 3 (residue 76). Two mutations were detected in the Brazzaville UF allele: a lysine (AAG) to methionine (ATG) substitution in exon 2 (residue 68) is responsible for the ultra-fast phenotype of this variant, while a tyrosine (TAT) to phenylalanine (TTT) substitution in exon 4 (residue 244) is not expected to alter the electrophoretic mobility of the encoded protein. These results indicate that the Gpdh UF alleles originate from different mutational events, and only two of them — Iowa UF and Netherlands UF — might share a common ancestry. The GPDH activity of the Iowa UF allele is intermediate between those of the Gpdh S and Gpdh F control stocks. The other Gpdh UF variants have lower activities than the controls: Xiamen UF -83%, Raleigh UF -80% and Brazzaville UF -73% of the Gpdh F control.
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