Comparative biochemistry of murine arylsulfatase B |
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Authors: | William L Daniel Michael S Caplan |
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Institution: | (1) Department of Genetics and Development, and School of Basic Medical Sciences, University of Illinois, 61801 Urbana, Illinois |
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Abstract: | Arylsulfatase B was purified 4500-fold from liver and kidney of C57BL/6J mice. Hepatic and renal arysulfatase B are apparently determined by a single structural locus; however, posttranslational modification introduces inter- and intratissue microheterogeneity. Partially purified enzyme from C57BL/6J, A/J, C3H/HeJ, and SWR/J mice has similar catalytic properties. The 4500-fold-purified arylsulfatase B from SWR/J and C3H/HeJ mice was more thermostable than that from C57BL/6J and A/J mice, strongly suggesting that the thermostability difference reflects an alteration of the primary structure of the enzyme. Thermal stability of arylsulfatase B was pH dependent and markedly influenced by buffer anion. Variation of thermostability did not appear accountable for the observed activity variation among these strains; however, this possibility cannot be rigorously excluded by presently available data. Thirty-five murine strains were found to possess the As-1
a
allele (thermostable enzyme), while As-1
b
was largely restricted to A and C57 strains.This research was supported by PHS Biomedical Sciences Research Support Grant RR-07030. |
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Keywords: | arylsulfatase house mouse genetic variation biochemical properties |
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