Skip to main content
Genetics logoLink to Genetics
. 1976 Mar;82(3):477–491. doi: 10.1093/genetics/82.3.477

Genetics of Murine Liver and Kidney Arylsulfatase B

William L Daniel 1
PMCID: PMC1213469  PMID: 5336

Abstract

Mice from 12 inbred strains were surveyed for variation of kidney and liver arylsulfatase levels. Kidney variation was due to differences in the activity of arylsulfatase B. Twofold higher activities of arylsulfatase B in SWR/J kidney compared to A/HeJ kidney were determined by an autosomal gene which may be identical to the structural gene for arylsulfatase B since the SWR/J enzyme was more heat-stable than the A/HeJ enzyme. C57BL/6J mice possessed twofold higher liver arylsulfatase levels than did A/HeJ mice. The major portion of this variation could be attributed to differences in arylsulfatase B, and appeared to be inherited in autosomal fashion. Although some evidence supports the existence of a major locus influencing liver arylsulfatase activity, this must be substantiated by further studies. Whatever the nature of the genetic factors involved, they do not appear to involve structural genes since no differences were discernible between the enzymes of the two strains relevant to Km, heat stability, electrophoretic mobility, pH optimum, activation energy, or response to several inhibitors. Furthermore, the rank ordering of strains on the basis of kidney arylsulfatase activity differed markedly from that which pertained to liver activity. Kidney arylsulfatase levels, but not brain or liver arylsulfatase activities, appear subject to androgenic influences.

Full Text

The Full Text of this article is available as a PDF (890.7 KB).

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Austin J., Armstrong D., Shearer L. Metachromatic form of diffuse cerebral sclerosis. V. The nature and significance of low sulfatase activity: a controlled study of brain, liver and kidney in four patients with metachromatic leukodystrophy (MLD). Arch Neurol. 1965 Dec;13(6):593–614. doi: 10.1001/archneur.1965.00470060029003. [DOI] [PubMed] [Google Scholar]
  2. DODGSON K. S., SPENCER B. Assay of sulfatases. Methods Biochem Anal. 1957;4:211–255. doi: 10.1002/9780470110201.ch6. [DOI] [PubMed] [Google Scholar]
  3. Erickson R. P. Erythrocytic nicotinamide-adenine dinucleotide phosphate levels and the genetic regulation of erythrocytic glucose 6-phosphate dehydrogenase activity in the inbred mouse. Biochem Genet. 1974 Jan;11(1):33–40. doi: 10.1007/BF00486617. [DOI] [PubMed] [Google Scholar]
  4. FISHMAN W. H., FARMELANT M. H. Effects of androgens and estrogens on beta-glucuronidase in inbred mice. Endocrinology. 1953 May;52(5):536–545. doi: 10.1210/endo-52-5-536. [DOI] [PubMed] [Google Scholar]
  5. Felton J., Meisler M., Paigen K. A locus determining beta-galactosidase activity in the mouse. J Biol Chem. 1974 May 25;249(10):3267–3272. [PubMed] [Google Scholar]
  6. Ganschow R. E., Schimke R. T. Independent genetic control of the catalytic activity and the rate of degradation of catalase in mice. J Biol Chem. 1969 Sep 10;244(17):4649–4658. [PubMed] [Google Scholar]
  7. Hutton J. J. Genetic regulation of glucose 6-phosphate dehydrogenase activity in the inbred mouse. Biochem Genet. 1971 Aug;5(4):315–331. doi: 10.1007/BF00485859. [DOI] [PubMed] [Google Scholar]
  8. Karl T. R., Chapman V. M. Linkage and expression of the Eg locus controlling inclusion of beta-glucuronidase into microsomes. Biochem Genet. 1974 May;11(5):367–372. doi: 10.1007/BF00486410. [DOI] [PubMed] [Google Scholar]

Articles from Genetics are provided here courtesy of Oxford University Press

RESOURCES