ISSN:
1573-4927
Schlagwort(e):
arylsulfatase
;
chondroitin-4-sulfatase
;
electrophoretic variants
;
house mouse
;
regulation
;
sulfatase
Quelle:
Springer Online Journal Archives 1860-2000
Thema:
Biologie
,
Chemie und Pharmazie
Notizen:
Abstract Arylsulfatase B (arylsulfate sulfohydrolase; EC 3.1.6.1) activities in C57BL/6J, SWR/J, and A/J mouse liver approximate a 5:3:1 ratio. Each enzyme was purified to apparent homogeneity, and the properties of the three purified enzymes were compared. The purified enzyme behaved as a monomer with an apparent molecular weight of 50,000. The purified enzyme catalyzed the hydrolysis ofp-nitrocatechol sulfate (pNCS), 4-methylumbelliferyl sulfate (4MUS), and chondroitin-4-sulfate (C4S) heptasaccharide. Purified SWR/J arylsulfatase B possessed a higher relative electrophoretic mobility atpH 4.0 than the A/J and C57BL/6J isozymes, and the SWR/J enzyme was more thermostable than either the C57BL/6J or the A/J enzyme. No differences were observed among the three enzymes with respect to their Michaelis constants for 4MUS and pNCS, isoelectric points, responses to inhibitors,pH optima, or electrophoretic mobilities atpH 8.3. The relativein vivo rates of synthesis of C57BL/6J, A/J, and SWR/J arylsulfatase B were comparable.
Materialart:
Digitale Medien
URL:
http://dx.doi.org/10.1007/BF02399408
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