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  • 1
    Electronic Resource
    Electronic Resource
    Leukocyte Sulfatidase for the Reliable Diagnosis of Metachromatic Leukodystrophy (1981)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 36 (1981), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: A simple assay technique for the determination of sulfatidase activity in leukocytes has been developed for the reliable diagnosis of metachromatic leukodystrophy (MLD). Sulfatide is tritiated in sphingosine and fatty acid by reduction with [3H]sodium borohydride in alkali in the presence of palladium chloride. This labeled natural substrate for aryl sulfatase A (AsA) is hydrolyzed by normal human leukocytes in 25 mwacetate buffer, pH 5.0, in the presence of 0.3% sodium taurodeoxycholate. The enzyme activity is greatly improved after dialysis, exhibiting better linearity with protein concentration. It is stimulated maximally by 5 mM-MnCl2 with an apparent Km of 0.17 MM for the substrate. Patients with MLD exhibited virtually no detectable sulfatidase activity although they had residual AsA activity that was measured with the synthetic substrate, p-nitrocatechol sulfate (NCS). Potential heterozygotes could be identified by the sulfatidase assay in instances where the NCS assay for AsA was inconclusive. Several individuals with levels of AsA activity characteristic of MLD, including a few healthy carriers and certain patients with unknown neurological diseases, were shown not to have MLD by the presence of measurable levels of sulfatidase in their leukocytes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1981.tb01648.x
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  • 2
    Electronic Resource
    Electronic Resource
    Congenital pontocerebellar atrophy in three patients: clinical, radiologic and etiologic considerations (1996)
    Springer
    Neuroradiology 38 (1996), S. 684-687 
    Details
    ISSN: 1432-1920
    Keywords: Key words Microcephaly ; Atrophy ; pontocerebellar
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract We report three patients with severe pontocerebellar atrophy (PCA) associated with a variable degree of cerebral atrophy. The clinical features consisted of progressive microcephaly, central hypotonia, visual impairment, abnormal eye movements and delayed psychomotor development. These are similar but not identical to the features of pontocerebellar hypoplasia type 2 described by Barth. The picture also differs from the classical form of autosomal dominant olivopontocerebellar atrophy. While in two patients the disease seemed to be genetic with highly suspicious autosomal recessive inheritance, the etiology in the third patient was probably nongenetic. We suggest that PCA is a morphologic entity with distinct radiologic features but variable clinical, pathophysiologic and etiologic backgrounds.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002340050334
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Isolation and characterization of the normal canine β-galactosidase gene and its mutation in a dog model of GM1-gangliosidosis (2000)
    Springer
    Journal of inherited metabolic disease 23 (2000), S. 593-606 
    Details
    ISSN: 1573-2665
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The acid β-galactosidase cDNA of Portuguese Water dogs was isolated and sequenced. The entire coding region of the gene consists of 2004 nucleotides encoding a protein of 668 amino acids. Its encoding sequence indicates approximately 86.5% identity at the nucleotide level and about 81% identity at the amino acid level with the encoding region of the human acid β-galactosidase gene. The deduced amino acid sequence contains a 24-amino-acid putative signal sequence, six possible glycosylation sites, and seven cysteine residues. A homozygous recessive mutation, causing canine GM1-gangliosidosis, was identified at nucleotide G200→A in exon 2 resulting in an Arg60→His (mutation R60H) amino acid substitution. The mutation creates a new restriction enzyme site for Pml1. Genotyping 115 dog samples for this acid β-galactosidase gene alteration readily distinguished affected homozygous recessives (n=5), heterozygous carriers (n=50) and normal homozygotes (n=60). DNA mutation analysis provided a method more specific than enzyme assay of β-galactosidase for determination of carriers.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1005630013448
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  • 4
    Electronic Resource
    Electronic Resource
    Characterization of α-mannosidase in feline mannosidosis (1988)
    Springer
    Journal of inherited metabolic disease 11 (1988), S. 3-16 
    Details
    ISSN: 1573-2665
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Acidic α-mannosidase deficiency has been identified in a family of Blue Persian cats. Characterization of the residual activity revealed that theK m for the substrate, 4-methylumbelliferyl-α-d-mannoside, increased approximately three-fold with a severe deficiency inV max (1–2%) in homogenates of liver and brain of affected cats compared with controls. The residual activity at pH 4.0 in liver homogenates from affected cats is very thermolabile at 51°C while the control activity is stable at this temperature for 1h. Subcellular fractionation of liver was performed from a control and diseased cat in order to compare the properties of the different α-mannosidases localized in these fractions. The residual activity present in the lysosomal fraction from diseased cat liver showed altered pH optimum, two-fold increase inK m with a severely reducedV max and increased thermolability compared with the activity in the lysosomal fraction from control liver. The thermal inactivation pattern andK m of the residual activity in the lysosomal fraction is different from the non-lysosomal α-mannosidase in the liver of the affected cat. This suggests that the residual activity in the lysosomal fraction of the liver from the affected cat is not due to contamination of non-lysosomal α-mannosidase in this fraction. Whether this residual activity represents the properties of the mutant enzyme or yet another minor normal component of lysosomes different from the major inactive mutant or absent lysosomal enzyme remains to be elucidated.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01800052
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    Paper (German National Licenses)
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