Abstract
Biochemical analyses of partially purified preparations of APH-4 and -6 (common allelic forms) and APH-2 and -10 (rare allelic forms) of D. melanogaster reveal that the two common forms are similar in all properties investigated except for pH optimum (8.0 vs. 8.5). The common and rare forms share certain properties in common but differ in that the common forms are more stable to heat and more sensitive to inhibition by inorganic phosphate. With respect to such properties as substrate preferences and K i values for inorganic phosphate, the common forms and APH-2 are similar to one another, whereas APH-10 is distinctly different. All four activities show preference for a phosphoaromatic compound as substrate, with O-phosphotyrosine being the best substrate of biological origin. Transphosphorylation, as related to these allelic forms of APH, is discussed.
Similar content being viewed by others
References
Axelrod, B. (1948). A new mode of enzymatic transfer. J. Biol. Chem. 1721.
Beckman, L., and Johnson, F. M. (1964). Variations in larval alkaline phosphatase controlled by Aph alleles in Drosophila melanogaster. Genetics 49829.
Dayan, J., and Wilson, I. (1964). The phosphorylation of tris by alkaline phosphatase. Biochim. Biophys. Acta 81620.
Fernley, H. N., and Walker, P. G. (1970). Inhibition of alkaline phosphatase by l-phenylalanine. Biochem. J. 116543.
Fishman, W. H., and Sie, H.-G. (1970). l-Homoarginine: An inhibitor of serum, “bone and liver” alkaline phosphatase. Clin. Chim. Acta 29339.
Fishman, W. H., Green, S., and Inglis, N. I. (1963). l-Phenylalanine: An organ specific, stereospecific inhibitor of human intestinal alkaline phosphatase. Nature 198685.
Harper, R. A., and Armstrong, F. B. (1972). Alkaline phosphatase of Drosophila melanogaster. I. Partial purification and characterization. Biochem. Genet. 675.
Johnson, F. M. (1966). Rapid single fly homogenization for the investigations of Drosophila enzymes. Drosophila Inform. Serv. 41193.
Lowry, O. H., Rosebrough, N. J., Farr, A. L., and Randall, R. J. (1951). Protein measurement with the Folin phenol reagent. J. Biol. Chem. 193265.
MacIntyre, R. J. (1966). Locus of the structural gene for 3rd larval instar alkaline phosphatase (Aph). Drosophila Inform. Serv. 4162.
Morton, R. K. (1958). The phosphotransferase activity of phosphatases. II. Studies with purified alkaline phosphomonoesterases and some substrate-specific phosphatases. Biochem. J. 70139.
Poulik, M. D. (1957). Starch gel electrophoresis in a discontinuous system of buffer. Nature 1801477.
Reid, T. W., and Wilson, I. B. (1971). Conformational isomers of alkaline phosphatase in the mechanism of hydrolysis. Biochemistry 10380.
Wallis, B. B., and Fox, A. S. (1968). Genetic and developmental relationships between two alkaline phosphatases in Drosophila melanogaster. Biochem. Genet. 2141.
Wilson, I., Dayan, J., and Cyr, K. (1964). Some properties of alkaline phosphatase from Escherichia coli. Transphosphorylation. J. Biol. Chem. 2394182.
Author information
Authors and Affiliations
Additional information
Paper No. 3892 of the Journal Series of the North Carolina State University Agricultural Experiment Station, Raleigh, North Carolina. This study was supported by Atomic Energy Commission Contract AT-(40-1-)-3980.
Rights and permissions
About this article
Cite this article
Harper, R.A., Armstrong, F.B. Alkaline phosphatase of Drosophila melanogaster. II. Biochemical comparison among four allelic forms. Biochem Genet 10, 29–38 (1973). https://doi.org/10.1007/BF00485746
Received:
Revised:
Issue Date:
DOI: https://doi.org/10.1007/BF00485746