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  • 1
    Electronic Resource
    Electronic Resource
    The most common mutation causing medium-chain acyl-CoA dehydrogenase deficiency is strongly associated with a particular haplotype in the region of the gene (1991)
    Springer
    Human genetics 〈Berlin〉 87 (1991), S. 425-428 
    Details
    ISSN: 1432-1203
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary RFLP haplotypes in the region containing the medium-chain acyl-CoA dehydrogenase (MCAD) gene on chromosome 1 have been determined in patients with MCAD deficiency. The RFLPs were detected after digestion of patient DNA with the enzymes BanII, PstI and TaqI and with an MCAD cDNA-clone as a probe. Of 32 disease-causing alleles studied, 31 possesed the previously publised A→G point-mutation at position 985 of the cDNA. This mutation has been shown to result in inactivity of the MCAD enzyme. In at least 30 of the 31 alleles carrying this G985 mutation a specific RFLP haplotype was present. In contrast, the same haplotype was present in only 23% of normal alleles (P≤3.4×10-18). These findings are consistent with the existence of a pronounced founder effect, possibly combined with biological and/or sampling selection.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00197161
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  • 2
    Electronic Resource
    Electronic Resource
    Localisation of RFLPs of the medium chain acyl-CoA dehydrogenase gene (1991)
    Springer
    Human genetics 〈Berlin〉 86 (1991), S. 537-538 
    Details
    ISSN: 1432-1203
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Six restriction fragment length polymorphisms (RFLPs) of the gene are described. Three of these are in linkage disequilibrium. Hybridisation with sub-probes allowed localisation of the RFLPs to different regions of the gene.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00194652
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  • 3
    Electronic Resource
    Electronic Resource
    Molecular characterization of medium-chain acyl-CoA dehydrogenase (MCAD) deficiency: identification of a lys329 to glu mutation in the MCAD gene, and expression of inactive mutant enzyme protein in E. coli (1991)
    Springer
    Human genetics 〈Berlin〉 86 (1991), S. 545-551 
    Details
    ISSN: 1432-1203
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary A series of experiments has established the molecular defect in the medium-chain acyl-coenzyme A (CoA) dehydrogenase (MCAD) gene in a family with MCAD deficiency. Demonstration of intra-mitochondrial mature MCAD indistinguishable in size (42.5-kDa) from control MCAD, and of mRNA with the correct size of 2.4 kb, indicated a point-mutation in the coding region of the MCAD gene to be disease-causing. Consequently, cloning and DNA sequencing of polymerase chain reaction (PCR) amplified complementary DNA (cDNA) from messenger RNA of fibroblasts from the patient and family members were performed. All clones sequenced from the patient exhibited a single base substitution from adenine (A) to guanine (G) at position 985 in the MCAD cDNA as the only consistent base-variation compared with control cDNA. In contrast, the parents contained cDNA with the normal and the mutated sequence, revealing their obligate carrier status. Allelic homozygosity in the patient and heterozygosity for the mutation in the parents were established by a modified PCR reaction, introducing a cleavage site for the restriction endonuclease NcoI into amplified genomic DNA containing G985. The same assay consistently revealed A985 in genomic DNA from 26 control individuals. The A to G mutation was introduced into an E. coli expression vector producing mutant MCAD, which was demonstrated to be inactive, probably because of the inability to form active tetrameric MCAD. All the experiments are consistent with the contention that the G985 mutation, resulting in a lysine to glutamate shift at position 329 in the MCAD polypeptide chain, is the genetic cause of MCAD deficiency in this family. We found the same mutation in homozygous form in 11 out of 12 other patients with verified MCAD deficiency.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00201539
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  • 4
    Electronic Resource
    Electronic Resource
    Oligonucleotide-priming methods for the chromosome-specific labelling of alpha satellite DNA in situ (1989)
    Springer
    Chromosoma 98 (1989), S. 259-265 
    Details
    ISSN: 1432-0886
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract It is demonstrated that either general staining of the centromeric regions of all primate chromosomes, or selective staining of the centromeric region of specific chromosomes, may be obtained in preparations of metaphase chromosomes by probing specifically for different regions within the alpha satellite DNA monomer. In order to exploit observed patterns of sequence variation within the monomer for this purpose, we have developed two new DNA analysis methods. In PRimed IN Situ labelling (PRINS), synthetic oligonucleotides derived from subsections of the monomer are hybridized to the chromosomes. The oligonucleotides then serve as primers for the in situ incorporation of biotin-labelled nucleotides catalysed by Klenow polymerase. Incorporated biotin is visualized with fluorescein isothiocyanate-labelled avidin (FITC-avidin). In Primed Amplification Labelling (PAL), biotin-labelled hybridization probes are produced in a polymerase chain reaction (PCR, Saiki et al. 1985), in which two synthetic oligonucleotide primers anneal within the same monomer. With the right choice of primers libraries of labelled probes derived from most monomers present as templates are produced. If DNA from a specific chromosome is used as template, then the resulting probe mixture gives stronger and more chromosome-specific signals in in situ hybridization experiments than does a cloned alpha satellite DNA probe derived from the same chromosome. The results obtained indicate that the alpha-repeat monomer is composed of regions with different degrees of chromosome specificity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00327311
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  • 5
    Electronic Resource
    Electronic Resource
    Close linkage between X-linked ectodermal dysplasia and a cloned DNA sequence detecting a two allele restriction fragment length polymorphism in the region Xp11-q12 (1986)
    Springer
    Human genetics 〈Berlin〉 74 (1986), S. 284-287 
    Details
    ISSN: 1432-1203
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary EDA (ectodermal dysplasia, anhidrotic) is an X-linked recessive disorder characterized by hypohidrosis, hypoor anodontia, and hypotrichosis. A possible linkage between the gene for EDA and a number of restriction fragment length polymorphisms (RFLPs) spread over the X chromosome was investigated in two Danish families segregating EDA. No recombination between the gene for EDA and our probe pTAK8, which detects a two allele polymorphism in the region Xp11-q12, was found in nine informative meiotic events (seven of which are phase known), giving a maximal lod score of 2.41 at a recombination fraction of 0.00. This juxtacentromeric location of the gene for EDA agrees well with the linkage data obtained with the other markers used in this study.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00282550
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  • 6
    Electronic Resource
    Electronic Resource
    Gas chromatographic mass spectrometric identification of N-dicarboxylmonoglycines (1978)
    Chichester : Wiley-Blackwell
    Biological Mass Spectrometry 5 (1978), S. 80-83 
    Details
    ISSN: 0306-042X
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: A number of N-dicarboxylmonoglycines of biological interest have been synthesized. They were characterized by means of mass spectrometry. Gas chromatography of the methyl esters of methylmalonyl-, succinyl-, glutaryl-, adipyl-, suberyl- and sebacylglycines showed a single sharp peak for each compound on Dexsil 300 and OV 17 columns. Methylene unit values and mass spectra of the six methyl esters are reported.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bms.1200050115
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  • 7
    Electronic Resource
    Electronic Resource
    N-acylglycines: Gas chromatographic mass spectrometric identification and determination in urine by selected ion monitoring (1979)
    Chichester : Wiley-Blackwell
    Biological Mass Spectrometry 6 (1979), S. 439-443 
    Details
    ISSN: 0306-042X
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Eleven biologically interesting N-acylglycines have been synthesized and the gas chromatographic and mass spectrometric properties of their trimethylsilyl derivatives studied. A sharp and reproducible gas chromatographic peak could be obtained for each N-acylglycine as the N, O-bis-(trimethylsilyl)-N-acylglycine. By the use of these derivatives a sensitive and specific selected ion monitoring method for the determination of N-acylglycines in human urine has been developed.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bms.1200061007
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  • 8
    Electronic Resource
    Electronic Resource
    Structural organization of the human short-chain acyl-CoA dehydrogenase gene (1997)
    Springer
    Mammalian genome 8 (1997), S. 922-926 
    Details
    ISSN: 1432-1777
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract. Short-chain acyl-CoA dehydrogenase (SCAD) is a homotetrameric mitochondrial flavoenzyme that catalyzes the initial reaction in short-chain fatty acid β-oxidation. Defects in the SCAD enzyme are associated with failure to thrive, often with neuromuscular dysfunction and elevated urinary excretion of ethylmalonic acid (EMA). To define the genetic basis of SCAD deficiency and ethylmalonic aciduria in patients, we have determined the sequence of the complete coding portion of the human SCAD gene (ACADS) and all of the intron-exon boundaries. The SCAD gene is approximately 13 kb in length and consists of 10 exons. Four polymorphic sites have previously been detected by sequencing of cDNA from fibroblasts of patients excreting elevated amounts of EMA. Three of these polymorphisms (321T/C, 990C/T, 1260G/C) are silent variants, while a 625G/A polymorphism results in an amino acid replacement and has been shown to be associated with ethylmalonic aciduria. From analysis of 18 unrelated Danish families, we show that the four SCAD gene polymorphisms constitute five allelic variants of the SCAD gene, and that the 625A variant together with the less frequent variant form of the three other polymorphisms (321C, 990T, 1260C) constitutes an allelic variant with a frequency of 22% in the general Danish population. Using fluorescence in-situ hybridization, we confirm the localization of the human SCAD gene to the distal part of Chromosome (Chr) 12 and suggest that the SCAD gene is a single-copy gene. The evolutionary relationship between SCAD and five other members of the acyl-CoA dehydrogenase family was investigated by two independent approaches that gave similar phylogenetic trees.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s003359900612
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