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  • 11
    Electronic Resource
    Electronic Resource
    Alternative molecular forms of erythrocyte catalase (1968)
    Springer
    Cellular and molecular life sciences 24 (1968), S. 119-121 
    Details
    ISSN: 1420-9071
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Zusammenfassung Katalase aus Erythrocyten vom Menschen (und Pferd) lässt sich säulenchromatographisch und elektrophoretisch in drei Fraktionen A, B und C auftrennen, wobei die Fraktionen A und B die Tendenz haben, in die Fraktion C überzugehen. Durch Chromatographie unter Ausschluss von Luftsauerstoff konnte gezeigt werden, dass die Katalase in den Erythrozyten in der Form A vorliegt. Setzt man das Hämolysat dagegen einige Zeit Luftsauerstoff aus, wird die Katalase bei der Chromatographie in Form C eluiert. SH-blockierende Reagentien verhindern die Umwandlung von A in C, während C mit Mercaptoäthanol zu A reduziert werden kann. Es wird angenommen, dass dem Übergang von Fraktion A in B und C eine Bildung von Disulfidbrücken zugrunde liegt und dass es sich bei den beobachteten alternativen Formen möglicherweise um Katalase-Konformere handelt.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02146931
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  • 12
    Electronic Resource
    Electronic Resource
    Mucopolysaccharidosis VII: β-Glucuronidase deficiency (1974)
    Springer
    Human genetics 〈Berlin〉 23 (1974), S. 149-158 
    Details
    ISSN: 1432-1203
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Description / Table of Contents: Zusammenfassung Bei einem 18 Monate alten Mädchen war die Aktivität des lysosomalen Enzyms β-D-Glucuronidase in gezüchteten Fibroblasten, Leukocyten und im Blutserum erheblich vermindert. Obligat heterozygote Anlageträger hatten in Serum und Leukocyten eine auf ca. 50% der Norm herabgesetzte Enzym-Aktivität. Klinisch fiel die Patientin durch Hurler-ähnliche Gesichtszüge auf, durch eine mäßige geistige Retardierung und Hepatosplenomegalie. Die Hornhäute waren spaltlampenmikroskopisch klar. Granulocyten des periphernen Blutbildes zeigten eine dichte Speicherung grober Alder-Reillyscher Einschlüsse. Im Urin wurden vermehrt saure Mucopolysaccharide ausgeschieden. Es handelte sich um eine Mucopolysaccharidose Typ VII. Das Krankheitsbild wird durch eine ungenügende Aktivität der β-D-Glucuronidase hervorgerufen. Saure Mucopolysaccharide können nicht abgebaut werden und häufen sich intralysosomal an.
    Notes: Summary An 18-month-old female showed a markedly decreased activity of the lysosomal enzyme β-D-glucuronidase in cultured fibroblasts, leucocytes, and serum. In obligate heterozygotes, the serum and leucocyte β-D-glucuronidase activity was decreased to approximately 50% of the control values. Clinically, the patient had a mild facial dysmorphism reminiscent of Hurler disease, moderate mental retardation, and hepatosplenomegaly. The corneae were clear. Peripheral granulocytes contained abundant, coarse Alder-Reilly granulations. The urinary excretion of acid mucopolysaccharides was increased. The disorder has been classified as mucopolysaccharidosis, type VII. It is assumed that this new mucopolysaccharidosis is caused by the defective action of β-glucuronidase which results in the faulty degradation and intralysosomal storage of acid mucopolysaccharides.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00282212
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  • 13
    Electronic Resource
    Electronic Resource
    The mucopolysaccharidoses: Inborn errors of glycosaminoglycan catabolism (1976)
    Springer
    Human genetics 〈Berlin〉 32 (1976), S. 233-255 
    Details
    ISSN: 1432-1203
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The mucopolysaccharidoses are genetic disorders of glycosaminoglycan metabolism. Patients with these diseases accumulate within the lysosomes of most tissues excessive amounts of dermatan and/or heparan sulfates, or of keratan sulfate. The clinical consequences of such glycosaminoglycan storage range from skeletal abnormalities to cardiovascular problems, and to motor and mental retardation. In all mucopolysaccharidoses, except Morquio disease, an excessive accumulation of sulfate-labeled glycosaminoglycans has been demonstrated in fibroblasts cultured from the patient's skin. It was subsequently shown that this was due to the deficiency of specific proteins which were named “corrective factors”, because their addition to the culture medium effected a normalization of the impaired glycosaminoglycan catabolism in the respective mucopolysaccharidosis fibroblasts. The investigation of the function of the corrective factors, and other studies, led to the identification of the enzymatic defect in each of the mucopolysaccharidoses. Seven lysosomal enzyme deficiencies are now recognized among this group of disorders. A classification of the diseases, according to the mutant gene products, reveals that there is considerable phenotypic variation not only between diseases, but also within several disease types. With the availability of the appropriate enzyme assays, the previous difficulties in diagnosing these disorders have now been overcome. Methods are also available for the prenatal diagnosis, and the detection of heterozygous individuals, in most of the mucopolysaccharidoses. Although correction of the metabolic defect through enzyme replacement has been achieved in tissue culture, many problems remain to be solved before such therapy may become applicable in the patients themselves.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00295816
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  • 14
    Electronic Resource
    Electronic Resource
    Normomorphic sialidosis in two female adults with severe neurologic disease and without sialyl oligosacchariduria (1986)
    Springer
    Human genetics 〈Berlin〉 74 (1986), S. 209-214 
    Details
    ISSN: 1432-1203
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Two female patients of German origin, aged 38 and 21 years, with myoclonus epilepsy and cerebellar ataxia, but without dysmorphic signs and dementia, were found to excrete normal amounts of sialyl oligosaccharides in their urine. The younger patient showed cherry red spots in her ocular fundi. The older patient had a brother with an autopsy-proven neuronal storage disease compatible with sialidosis, and in her rectal biopsy lamellar inclusion bodies were detected. Enzyme assays in cultured fibroblasts of both patients revealed a profound but incomplete deficiency of oligosaccharide sialidase activity and normal β-galactosidase activity. Adult sialidosis was diagnosed in both patients. In their fibroblasts, moderate elevations of bound sialic acid could also be measured. The small residual sialidase activity, which in the older patient had a normal KM value, is considered responsible for the late onset and slow clinical course of the disease. It is concluded that in adult sialidosis the extraneural storage process can be difficult to demonstrate in terms of metabolite accumulation or excretion during the course of intraneuronal storage.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00282535
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  • 15
    Electronic Resource
    Electronic Resource
    Über die celluläre Verteilung der Katalase im Blut homozygoter und heterozygoter Defektträger (Akatalasie) (1966)
    Springer
    Human genetics 〈Berlin〉 3 (1966), S. 50-63 
    Details
    ISSN: 1432-1203
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Description / Table of Contents: Zusammenfassung Auf Grund der sehr ungleichen Methämoglobinbildung bei Peroxideinwirkung lassen sich katalasehaltige und katalasefreie Erythrocyten im Ausstrichpräparat (behandelt nach Kleihauer u. Betke) voneinander unterscheiden. Mit diesem Verfahren haben sich bei der Untersuchung von Blutproben heterozygoter Defektträger keine Anhaltspunkte für das Bestehen zweier Zellpopulationen finden lassen. Dagegen weisen 0,5–1,0% aller Erythrocyten im Blut homozygoter Defektträger einen annähernd normalen Katalasegehalt auf. Durch Fraktionierung der roten Blutzellen auf Grund ihrer Dichte (bzw. nach Alter) läßt sich zeigen, Daß zwischen Katalaseaktivität und Reticulocytengehalt direkte Proportionalität besteht. Bei drei Akatalasiefällen verhält sich (die durch Extrapolation errechnete) Katalaseaktivität in Reticulocyten und Erythrocyten wie ca. 300:1. Die im Gegensatz zur Norm massive Aktivitätsabnahme ist möglicherweise auf die Instabilität der bei diesen Defektträgern vorkommenden Enzymvariante zurückzuführen.
    Notes: Abstract Normal (catalase containing) and acatalatic red cells can be distinguished in smears (prepared by the method of Kleihauer and Betke) by means of their unequal methemoglobin content produced by the action of peroxide. An investigation of blood samples of heterozygous acatalatic subjects by this method has shown no evidence for the existence of two cell population. On the other hand 0.5–1.0% of all erythrocytes in the blood of homozygous cases show an approximately normal catalase content. On analysis of red cell fractions of different density (age) it can be shown that there is a direct proportionality between catalase activity and the number of reticulocytes. In three cases of acatalasia, catalase activity in reticulocytes and erythrocytes as calculated by extrapolation differs by a ratio of approximately 300:1. This decrease in catalase activity, which is contrary to that found in normal individuals, is possibly due to the instability of a variant enzyme occuring in acatalatic subjects.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00273019
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  • 16
    Electronic Resource
    Electronic Resource
    N-Acetylneuraminic acid storage disease (1985)
    Springer
    Human genetics 〈Berlin〉 71 (1985), S. 155-159 
    Details
    ISSN: 1432-1203
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Increased amounts of free sialic acid were found in body fluids, leukocytes, cultured fibroblasts, and liver tissue of a four-year-old boy with mental retardation, ataxia, and clinical and radiologic findings of a mild mucopolysaccharidosis. A diagnosis of Salla disease was made though in contrast to earlier reports, recurrent upper respiratory infections and hepatosplenomegaly were present already in infancy, and skeletal abnormalities of dysostosis multiplex were found in early childhood. Free sialic acid in the urine was identified as N-acetylneuraminic acid by 1H-NMR spectroscopy. Sialidase activities were normal. Increased amounts of bound sialic acid were found in liver and cultured fibroblasts and were attributed to an intracellular inhibition of sialyloligosaccharide-degrading neuraminidase by excessive amounts of free neuraminic acid. The molecular basis of N-acetylneuraminic acid storage disease is unknown but may be related to a defective transport mechanism preventing neuraminic acid from leaving the lysosomal compartment.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00283373
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  • 17
    Electronic Resource
    Electronic Resource
    S3.7 Lysosomal and plasma membrane-bound ganglioside GM3-sialidases of human neuroblastoma cells during cell proliferation (1993)
    Springer
    Glycoconjugate journal 10 (1993), S. 243-243 
    Details
    ISSN: 1573-4986
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01209878
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  • 18
    Electronic Resource
    Electronic Resource
    S3.6 Effects of ganglioside sialidase inhibitors on proliferation and differentiation of human neuroblastoma cells (1993)
    Springer
    Glycoconjugate journal 10 (1993), S. 243-243 
    Details
    ISSN: 1573-4986
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01209877
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  • 19
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    The Defect in the Hunter Syndrome: Deficiency of Sulfoiduronate Sulfatase (1973)
    National Academy of Sciences
    Details
    Publication Date: 1973-07-01
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
    Published by National Academy of Sciences
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  • 20
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    Alternative molecular forms of erythrocyte catalase (1968)
    Springer
    Details
    Publication Date: 1968-02-01
    Print ISSN: 0014-4754
    Topics: Biology , Medicine
    Published by Springer
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