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Activity differences between acid phosphatase allozyme variants of Drosophila virilis: Differences in intracellular localization of allozymes

Published online by Cambridge University Press:  14 April 2009

Sumiko Narise
Sumiko Narise
Affiliation:
Biological Laboratory, Faculty of Science, Josai University, Sakado, Saitama 350–02, Japan
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Three acid phosphatase allozyme strains (Acph-1, Acph-2 and Acph-4) of Drosophila virilis show large differences of enzyme activity when examined by means of starch gel electrophoretic technique, Acph-4 strain showing approximately four times the activity of Acph-1 and twice that of Acph-2, as reported previously (Narise, 1976). Crude extract difference between Acph-4 and Acph-1 strains is less than twofold and this compared with larger differences in supernatants. Cell fractionation and density gradient centrifugation demonstrated that the acid phosphatase resides mainly in lysosomes and becomes soluble in part during preparation without structural damage to lysosomes. The solubility of the allozymes from lysosomes was variable among the three strains. ACPH4 allozyme was released in the highest degree. However, the release-rate of other lyso-somalenzymes, such as α-glucosidase, β-galactosidase and β-glucuronidase was similar among these strains. These results suggest that the strain variation in ability of the allozymes to be incorporated into lysosomes is due to the allozymes themselves, not due to alteration in the lysosomes.

Type
Research Article
Information
Genetics Research , Volume 45 , Issue 2 , April 1985 , pp. 143 - 153
Copyright
Copyright © Cambridge University Press 1985

References

REFERENCES

Abraham, I. & Doane, W. W. (1978). Genetic regulation of tissue-specific expression of Amylase structural genes in Drosophila melanogaster. Proceedings of the National Academy of Sciences of U.S.A. 75, 4446–4450.CrossRefGoogle ScholarPubMed
Bock, R. M. & Ling, N. S. (1954). Devices for gradient elution in chromatography. Analytical Chemistry 26, 1543–1546.CrossRefGoogle Scholar
DeAraujo, P. S., Mies, V. & Miranda, O. (1976). Subcellular distribution of low- and high-molecular-weight acid phosphatases. Biochimica et Biophysica Ada 452, 121–130.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
Doane, W. W. (1969). Amylase variants in Drosophila melanogaster: Linkage studies and characterization of enzyme extracts. Journal of Experimental Zoology 171, 321–342.CrossRefGoogle ScholarPubMed
Gibson, J. B. & Miklovich, R. (1971). Modes of variation in alcohol dehydrogenase in Drosophila melanogaster. Experimentia 27, 99–100.CrossRefGoogle ScholarPubMed
Gibson, J. B. (1972). Differences in the number of molecules produced by two allelic electrophoretic enzyme variants in D. melanogaster. Experimentia 28, 975–976.CrossRefGoogle ScholarPubMed
Hickman, S. & Neufeld, E. F. (1972). A hypothesis for I-cell disease: defective hydrolases that do not enter lysosomes. Biochemical and Biophysical Research Communications 49, 992–999.CrossRefGoogle Scholar
Hicky, D. A. (1977). Selection for amylase allozymes in Drosophila melanogaster. Evolution 31, 800–804.CrossRefGoogle Scholar
Hicky, D. A. (1981). Regulation of amylase activity in Drosophila melanogaster: Variation in the number of enzyme molecules produced by different amylase genotypes. Biochemical Genetics 19, 783–796.CrossRefGoogle Scholar
Kaplan, A., Achord, D. T. & Sly, W. S. (1977). Phosphohexosyl components of a lysosomal enzyme are recognized by pinocytosis receptors on human fibroblasts. Proceedings of the National Academy of Sciences of U.S.A. 74, 2026–2030.CrossRefGoogle ScholarPubMed
King, T. E. (1967). Preparation of succinate dehydrogenase and reconstitution of succinate oxidase. Methods in Enzymology 10, 322–331.CrossRefGoogle Scholar
McDonald, J. F., Chambers, G. K., David, J. & Ayala, F. J. (1977). A adaptive response due to changes in gene regulation: A study with Drosophila. Proceedings of the National Academy of Sciences of U.S.A. 74, 4562–4566.CrossRefGoogle ScholarPubMed
McDonald, J. F. & Ayala, F. J. (1978). Genetic and biochemical basis of enzyme activity variation in natural populations. 1. Alcohol dehydrogenase in Drosophila melanogaster. Genetics 89, 371–388.CrossRefGoogle ScholarPubMed
Narise, S. (1976). Biochemical study on enzyme produced by alleles at the acid phosphatase locus in Drosophila virilis. The Japanese Journal of Genetics 51, 428 (in Japanese).Google Scholar
Narise, S. (1983). Activity difference among acid phosphatase allozymes from D. virilis. Drosophila Information Service 59, 95–96.Google Scholar
Narise, S. (1984). Purification and properties of acid phosphatase from Drosophila virilis. Insect Biochemistry 14, 473–480.CrossRefGoogle Scholar
Natowicz, M. R., Chi, M. M.-Y., Lowry, O. H. & Sly, W. S. (1979). Enzymatic identification of mannose 6-phosphate on the recognition marker for receptor-mediated pinocytosis of β-glucuronidase by human fibroblasts. Proceedings of the National Academy of Sciences of U.S. A 76, 4322–4326.CrossRefGoogle ScholarPubMed
Neuberger, A., Gottschalk, A., Marshall, R. D. & Spiro, R. G. (1972). Carbohydrate-peptide linkages in glycoproteins and methods for the elucidation. In Glycoproteins, Part A (ed. Gottschalk, A.). pp. 450–490. Amsterdam: Elsevier Publishing Company.Google Scholar
Neufeld, E. F., Lim, T. W. & Shapiro, L. J. (1975). Inherited disorders of lysosomal metabolism. Annual Review of Biochemistry 44, 357–376.CrossRefGoogle ScholarPubMed
Ohba, S. (1977). Population genetics (in Japanese). UP Biology Series 19, 99–104. Tokyo: Tokyo University Press.Google Scholar
Ostrowski, W., Wasyl, Z., Weber, M., Guminska, M. & Lechter, E. (1970). The role of neuraminic acid in the heterogeneity of acid phosphomonoesterase from the human prostate gland. Biochimica et Biophysica Acta 221, 297–306.CrossRefGoogle ScholarPubMed
Pipkin, S. B. & Hewitt, N. E. (1972). Variation of alcohol dehydrogenase levels in Drosophila species hybrids. The Journal of Heredity 63, 267–270.CrossRefGoogle Scholar
Powell, J. R. & Lichtenfels, J. M. (1979). Population genetics of Drosophila amylase. I. Genetic control of tissue-specific expression of D. pseudoobscura. Genetics 92, 603–612.CrossRefGoogle ScholarPubMed
Rasmuson, B., Nilson, L. R., Rasmuson, M. & Zeppezauer, E. (1966). Effect of heterozygosity on alcohol dehydrogenase (ADH) activity in Drosophila melanogaster. Hereditas 56, 313–316.CrossRefGoogle Scholar
Robinson, D. & Stirling, J. L. (1968). N-Acetyl-β-glucosaminidases in human spleen. The Biochemical Journal 107, 321–327.CrossRefGoogle Scholar
Sawicki, J. A. & MacIntyre, R. J. (1978). Localization at the ultrastructural level of maternally derived enzyme and determination of the time of paternal gene expression of acid phosphatase-1 in Drosophila melanogaster. Developmental Biology 63, 47–58.CrossRefGoogle Scholar
Shaw, C. R. & Prasad, R. (1970). Starch electrophoresis of enzymes - A complication of recipes. Biochemical Genetics 4, 297–320.CrossRefGoogle Scholar
Tejima, T. & Ohba, S. (1981). Genetic regulation of amylase activity in Drosophila virilis. I. Activity variation among laboratory strains. The Japanese Journal of Genetics 56, 457–468.CrossRefGoogle Scholar
Ward, R. D. (1975). Alcohol dehydrogenase activity in Drosophila melanogaster: a quantitative character. Genetical Research, Cambridge 26, 81–93.CrossRefGoogle ScholarPubMed