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Strain variation in spermatozoal glycosidases in inbred mice

Published online by Cambridge University Press:  14 April 2009

Steven J. Self ,
Bryan G. Winchester  and
James R. Archer
Steven J. Self
Affiliation:
Department of Biochemistry, Queen Elizabeth College (University of London), Campden Hill Road, London W8 7AH G. D. Searle & Co. Ltd., Research Division, P.O. Box 53, Lane End Road, High Wycombe, Bucks. HP12 4HL
Bryan G. Winchester
Affiliation:
Department of Biochemistry, Queen Elizabeth College (University of London), Campden Hill Road, London W8 7AH
James R. Archer
Affiliation:
G. D. Searle & Co. Ltd., Research Division, P.O. Box 53, Lane End Road, High Wycombe, Bucks. HP12 4HL
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Summary

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Ten glycosidases were measured in suspensions of spermatozoa from the vasa deferentia of two inbred mouse strains and their intercrosses. Eight of these glycosidases were associated with the sperm cells and all of these showed genetical variation between the strains except α-l-fucosidase with optimal activity at pH 5·4. In contrast liver enzyme activities showed no significant variation except α-l-fucosidase. Genetic studies indicated that the variation of spermatozoal β-d-hexosaminidase, α-d-mannosidase, α-l-fucosidase and β-d-galactosidase are inherited at autosomal loci and α-d-galactosidase variation shows X-linked inheritance. We propose a new provisional gene symbol (Afuc-2) for a spermatozoal variant of α-l-fucosidase.

Type
Research Article
Information
Genetics Research , Volume 32 , Issue 2 , October 1978 , pp. 183 - 193
Copyright
Copyright © Cambridge University Press 1978

References

REFERENCES

Allison, A. C. & Hartree, E. F. (1970). Lysosomal enzymes in the acrosome and their possible role in fertilization. Journal of Reproduction and Fertility 21, 501–515.Google Scholar
Bullock, S. (1975). Glycosidases of the mammalian male reproductive tract. Ph.D. thesis, Queen Elizabeth College, University of London.Google Scholar
Conchie, J., Findlay, J. & Levvy, G. A. (1959). Mammalian glycosidases – distribution in the body. Biochemical Journal 71, 318–325.CrossRefGoogle ScholarPubMed
Conchie, J. & Mann, T. (1957). Glycosidases in mammalian sperm and spermatozoa. Nature 179, 1190–1191.CrossRefGoogle Scholar
Dizik, M. & Elliott, R. W. (1977). A gene apparently determining the extent of sialylation of lysosomal α-mannosidase in mouse liver. Biochemical Genetics 15, 31–46.CrossRefGoogle ScholarPubMed
Erickson, R. P. (1976). Strain variation in spermatozoal β-glucuronidase in mice. Genetical Research 28, 139–145.Google Scholar
Erickson, R. P. (1977). Genetic control of β-glucuronidase in murine spermatozoa. Experientia 33, 315–316.Google Scholar
Erickson, R. P. & Krzanowska, H. (1974). Differences in hyaluronidase among inbred strains of mice and their possible significance for variations in fertility. Journal of Reproduction and Fertility 39, 101–104.CrossRefGoogle Scholar
Felton, J., Meisler, M. & Paigen, K. (1974). A locus determining β-galactosidase activity in the mouse. Journal of Biological Chemistry 249, 3267–3272.CrossRefGoogle ScholarPubMed
Lalley, P. A. & Shows, T. B. (1974). Lysosomal and microsomal β-glucuronidase: genetic variant alters electrophoretic mobility of both hydrolases. Science 185, 442–444.Google Scholar
Lowry, O. H., Rosebrough, N. J., Farr, A. L. and Randall, R. J. (1951). Protein measurement with the Folin phenol reagent. Journal of Biological Chemistry 193, 265–275.CrossRefGoogle ScholarPubMed
Lusis, A. J. & West, J. D. (1976). X-linked inheritance of a structural gene for α-galactosidase in Mus musculus. Biochemical Genetics 14, 849–855.CrossRefGoogle ScholarPubMed
Majumder, G. C., Lessin, S. & Turkington, R. W. (1975). Hormonal regulation of isoenzymes of N-acetyl-β-glucosaminidase and β-galactosidase during spermatogenesis in the rat. Endocrinology 96, 890–897.CrossRefGoogle ScholarPubMed
Majumder, G. C. & Turkington, R. W. (1974). Acrosomal and lysosomal isoenzymes of β-galactosidase and N-acetyl-β-glucosaminidase in rat testis. Biochemistry 13, 2857–2864.CrossRefGoogle ScholarPubMed
Mathur, R. S. (1971). Histo-enzymological observations on spermatozoa of inbred strains of mice. Journal of Reproduction and Fertility 27, 5–11.CrossRefGoogle ScholarPubMed
McIlvaine, T. C. (1921). A buffer solution for colorimetric comparison. Journal of Biological Chemistry 4, 183–186.CrossRefGoogle Scholar
Morrow, A. G., Greenspan, E. M. & Carroll, D. M. (1949). Liver glucuronidase activity of inbred mouse strains. Journal of the National Cancer Institute 10, 657–661.Google Scholar
Sanderson, A. R. (1965). Quantitative titration, kinetic behaviour and inhibition of cytotoxic mouse isoantisera. Immunology 9, 287–300.Google ScholarPubMed
Seyedyazdani, R. & Lundin, L. G. (1973). Association between β-galactosidase activities and coat colour in mice. Journal of Heredity 64, 295–296.CrossRefGoogle ScholarPubMed
Swank, R. T. & Paigen, K. (1973). Biochemical and genetic evidence for a macromolecular β-glucuronidase complex in microsomal membranes. Journal of Molecular Biology 77, 371–389.CrossRefGoogle ScholarPubMed
Swank, R. T., Paigen, K. & Ganschow, R. E. (1973). Genetic control of glucuronidase induction in mice. Journal of Molecular Biology 81, 225–243.Google Scholar
Wigzell, H. (1965). Quantitative titrations of mouse H-2 antibodies using 51Cr labelled target cells. Transplantation 3, 423–431.Google Scholar
Zaneveld, L. J. D., Polakoski, K. L. & Schumacher, G. F. B. (1973). Properties of acrosomal hyaluronidase from bull spermatozoa. Journal of Biological Chemistry 248, 564–570.CrossRefGoogle ScholarPubMed