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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Cellular and molecular life sciences 39 (1983), S. 740-742 
    ISSN: 1420-9071
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary SWR/J mice posses high arylsulfatase C, estrone sulfatase, and dehydroepiandrosterone sulfatase activities in liver, spleen and kidney compared to A/J mice. This internstrain activity variation appears to be determined by at least 1 autosomal gene. Murine arylsulfatase C activity occurs in both hydrophobic and hydrophilic forms which differ with respect to certain biochemical properties and exhibit different subcellular distributions. The hydrophilic isozyme is a major component in kidney and brain extracts and a minor isozyme in liver and spleen extracts. The hydrophobic arylsulfatase C isozyme appears to be identical to steroid sulfatase. The hydrophilic arylsulfatase C isozyme does not possess steroid sulfatase activity; however, hydrophilic and hydrophobic arylsulfatase C share certain properties, suggesting that they may be structurally related. The autosomal gene(s) affects both arylsulfatase isozymes.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Cellular and molecular life sciences 42 (1986), S. 150-151 
    ISSN: 1420-9071
    Keywords: Arylsulfatase A ; arylsulfatase B ; 4-methylumbelliferyl sulfate ; rodent ; bovine
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Rodent and bovine arylsulfatase B hydrolyze 4-methylumbelliferyl sulfate (4MUS) 10- to 30-fold more efficiently than arylsulfatase A. Therefore, 4MUS grossly underestimates arylsulfatase A activity in the presence of excess arylsulfatase B.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Cellular and molecular life sciences 38 (1982), S. 73-75 
    ISSN: 1420-9071
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Murine brain possesses an anionic form of arylsulfatase B which accounts for approximately 12–16% of nonmicrosomal arylsulfatase activity. This isozyme is antigenically similar to cationic arylsulfatase B, displays a similar developmental profile, and can be converted to a form resembling the cationic species by prior treatment with neuraminidase.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 27 (1976), S. 0 
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Springer
    Cellular and molecular life sciences 35 (1979), S. 309-310 
    ISSN: 1420-9071
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary A method has been developed for the assay of arylsulfatase C in tissue extracts containing arylsulfatases A and B. Significant variation of enzyme activity was observed among 26 inbred murine strains. Activity differences were apparent at all stages evaluated between 1 and 70 days postnatal age. Arylsulfatase C from representative high- and low-activity strains exhibited similar Michaelis constants, temperature optima, pH optima, thermostabilities and inhibitor profiles.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Springer
    Cellular and molecular life sciences 43 (1987), S. 1209-1211 
    ISSN: 1420-9071
    Keywords: Arylsulfatase B ; lysosomal enzymes ; mouse ; sulfatase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Arylsulfatase B activity levels were approximately 2–3-fold higher in adult C57BL/6J liver and kidney compared to corresponding tissues from A/J inbred mice. In vivo incorporation of tritiated leucine into C57BL/6J hepatic arylsulfatase B reached a maximum approximately 15 h after injection. The label was cleared from C57BL/6J arylsulfatase B with an apparent half-life of 36 h. The relative rates of synthesis of C57BL/6J and A/J arylsulfatase B were similar; however, the A/J enzyme was cleared more rapidly from liver tissue. C57BL/6J kidney arylsulfatase B appeared to be synthesized at a 2–3-fold higher rate than the corresponding A/J enzyme. These trends suggest genetic regulation of arylsulfatase B is effected through different means in liver and kidney from adult mice of these two inbred strains.
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    Springer
    Biochemical genetics 14 (1976), S. 933-952 
    ISSN: 1573-4927
    Keywords: β-galactosidase ; kidney isoenzymes ; molecular properties ; mouse ; inheritance ; tissue variation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Two closely linked regulatory genes have been reported to control activity levels of β-galactosidases in murine tissues. The specific effects of these genes on murine glycolipid metabolism have not been elucidated. A/HeJ kidney 4-methylumbelliferyl-β-galactosidase exhibited lower thermostability than the corresponding C57BL/6J and SWR/J enzymes. This altered response to heat segregated with the Bgs hallele among progeny derived from backcrosses of F1 (A/HeJ; SWR/J) mice to the respective parental strains. Restriction of the heat-sensitive A/HeJ β-galactosidase to kidney tissue suggests that it is not determined by the Bgs locus, since the latter appears to be expressed in all tissues. More likely, the Bgs region of chromosome 9 contains a gene cluster consisting of a number of regulatory and structural loci. The proposed structural genes share affinity for the artificial substrates commonly employed for their assay but may differ in their relative affinities for glycosphingolipid substrates. Presence of the Bgs hallele results in an increase of kidney GM1-ganglioside-β-galactosidase; however, galactosylceramide-β-galactosidase appears unaffected by this allele.
    Type of Medium: Electronic Resource
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