Purification and identification of the essential ionizable groups of honeybee, Apis mellifera L., trehalase

Bioscience, Biotechnology and Biochemistry

Volumn 65, Issue 12, 2001, Pages 2657-2665

  Lee, Jin Ha ^a   Tsuji, Masahisa ^a   Nakamura, Mitsuru ^a   Nishimoto, Mamoru ^a   Okuyama, Masayuki ^a   Mori, Haruhide ^a   Kimura, Atsuo ^a   Matsui, Hirokazu ^a   Chiba, Seiya ^a  

^a HOKKAIDO UNIVERSITY   (Japan)

Author keywords

, trehalose; , trehalose; Apis mellifera; Essential ionizable group; Honeybee trehalase

Indexed keywords

APIS MELLIFERA;

GLUCOSE; TREHALASE; TREHALOSE;

ANIMAL; ARTICLE; BEE; BIOSYNTHESIS; CHEMISTRY; ENZYME SPECIFICITY; GAS CHROMATOGRAPHY; GEL CHROMATOGRAPHY; HYDROLYSIS; ISOLATION AND PURIFICATION; KINETICS; METABOLISM; PH; POLYACRYLAMIDE GEL ELECTROPHORESIS; TEMPERATURE;

ANIMALS; BEES; CHROMATOGRAPHY, GAS; CHROMATOGRAPHY, GEL; ELECTROPHORESIS, POLYACRYLAMIDE GEL; GLUCOSE; HYDROGEN-ION CONCENTRATION; HYDROLYSIS; KINETICS; SUBSTRATE SPECIFICITY; TEMPERATURE; TREHALASE; TREHALOSE;

EID: 0035752068     PISSN: 09168451     EISSN: None     Source Type: Journal    
DOI: 10.1271/bbb.65.2657     Document Type: Article

References (35)

1. Hehre, E. J., Sawai, T., Brewer, C. F., Nakano, M., and Kanda, T., Trehalase: stereocomplementary hydrolytic and glucosyl transfer reactions with α- and β-glucosyl fluoride. Biochemistry, 21, 3090-3097 (1982).
2. Weiser, W., Lehmann, J., Chiba, S., Matsui, H., Brewer, C. F., and Hehre, E. J., Steric course of the hydration of D-gluco-octenitol catalyzed by α-glucosidases and by trehalase. Biochemistry, 27, 2294-2300 (1988).
3. Hey, A. E. and Elbein, D. A., Partial purification and properties of a trehalase from Streptomyces hygroscopicus. J. Bacteriol., 96, 105-110 (1968).
4. Vijayakumar, P., Ross, W., and Reese, E. T., α,α-Trehalase of Trichoderma reesei. Can. J. Microbiol., 24, 1280-1283 (1978).
5. Huston, D. H. and Manners, D. J., Studies on carbohydrate-metabolizing enzymes: the hydrolysis of α-glucosides, including nigerose by alfalfa and other higher plants. Biochem. J., 94, 783-789 (1965).
6. Alexander, A. G., Studies on trehalase in Saccharum spp. leaf and storage tissues. Plant Cell Physiol., 14, 157-168 (1973).
7. Saito, S., Trehalase of silkworm, Bombyx mori: purification and properties of the enzyme. J. Biochem., 48, 101-109 (1960).
8. Talbot, B. G. and Huber, R. E., Partial purification, stabilization and characterization of adult honey bee midgut trehalase and a new trehalase specific disc gel stain method. Insect Biochem., 5, 337-347 (1975).
9. Sacktor, B., Trehalase and the transport of glucose in the mammalian kidney and intestine. Proc. Natl. Acad. Sci. USA, 60, 1007-1014 (1968).
10. Nakano, M., Sumi, Y., and Miyakawa, M., Purification and properties of trehalase from rat intestine. J. Biochem., 81, 1041-1049 (1977).
11. Galand, G., Purification and characterization of kidney and intestinal brush-border membrane trehalases from the rabbit. Biochim. Biophys. Acta, 789, 10-19 (1984).
12. Lefebvre, Y. A. and Huber, R. E., Solubilization, purification, and properties of trehalase from honeybee (Apis mellifera). Arch. Biochem. Biophys., 140, 514-518 (1970).
13. Talbot, B. G., Muir, J. G., and Huber, R. E., Properties of a free and a solubilized form of bound α,α-trehalase purified from honey bee thorax. Can. J. Biochem., 53, 1106-1117 (1975).
14. Gutierrez, C., Ardourel, M., Bremer, E., Middendorf, A., Boos, W., and Ehmann, U., Analysis and DNA sequence of the osmoregulated treA gene encoding the periplasmic trehalase of Escherichia coli K12. Mol. Gen. Genet., 217, 347-354 (1989).
15. Ruf, J., Wacker, H., James, P., Maffia, M., Seiler, P., G., von Kieckebusch, A., Semenza, G., and Mantei, N., Rabbit small instestinal trehalase: purification, cDNA cloning, expression, and verification of glycosylphosphatidylinositol anchoring. J. Biol. Chem., 265, 15034-15039 (1990).
16. Su, Z., Sato, Y., and Yamashita, O., Purification, cDNA cloning and northern blot analysis of trehalase of pupal midgut of the silkworm, Bombyx mori. Biochim. Biophys. Acta, 1173, 217-224 (1993).
17. Ogawa, M. and Ariyoshi, U., The purification and proproteins of trehalase from lady beetle, Harmonia axyridis. Insect Biochem., 11, 397-400 (1981).
18. Defaye, J., Driguez, H., and Henrisat, B., Stereochemistry of the hydrolysis of α,α-trehalose by trehalase, determined by using a labelled substrate. Carbohydr. Res., 124, 265-273 (1983).
19. Block, R. and Burger, M. M., A rapid procedure for derivatizing agarose with a variety of carbohydrate: its use for affinity chromatography of lectins. FEBS Lett., 44, 286-289 (1974).
20. Kimura, A., Takewaki, S., Matsui, H., Kubota, M., and Chiba, S., Allosteric properties, substrate specificity, and subsite affinities of honeybee α-glucosidase I. J. Biochem., 107, 762-768 (1990).
21. Dayhoff, M. O., Perlmann, G. E., and MacInnes, D. A., Partial specific volumes, in aqueous solution, of three proteins. J. Am. Chem. Soc., 74, 2515-2517 (1952).
22. Bradford, M. M., A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem., 72, 248-254 (1976).
23. Bearden Jr., J. C., Quantitation of submicrogram quantities of protein by an improved protein-dye binding assay. Biochim. Biophys. Acta, 533, 525-529 (1978).
24. Dubois, M., Gilles, R., Hamilton, J. K., Rebers, P. A., and Smith, F., Calorimetric method for determination of sugars and related substances. Anal. Chem., 28, 350-356 (1956).
25. Takewaki, S., Chiba, S., Kimura, A., Matsui, H., and Koike, Y., Purification and properties of α-glucosidases of the honey bee Apis mellifera L. Agric. Biol. Chem., 44, 731-740 (1980).
26. King, T. P., Separation of proteins by ammonium sulfate gradient solubilization. Biochemistry, 11, 367-371 (1972).
27. Chiba, S., Kimura, A., and Matsui, H., Quantitative study of anomeric forms of glucose by α-glucosidase and glucoamylase. Agric. Biol. Chem., 47, 1741-1746 (1983).
28. Reisfeld, R. A., Lewis, U. J., and Williams, D. E., Disk electrophoresis of basic proteins and properties of polyacrylamide gels. Nature, 195, 281-283 (1962).
29. Laemmli, U. K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685 (1970).
30. Labat, J., Baumann, F., and Courtois, J-E., Hydrolyses du trehalose par la trehalase du rein de porc: configuration anomerique α du D-glucose libere. Carbohydr. Res., 26, 341-349 (1973).
31. Clifford, K. H., Stereochemistry of the hydrolysis of trehalose by the enzyme trehalase prepared from flesh fly Sarcophage barbata. Eur. J. Biochem., 106, 337-340 (1980).
32. Nakano, M., Brewer, C. F., Kasumi, T., and Hehre, E. J., Steric course of the hydrolysis of α,α-trehalose and α-D-glucosyl fluoride catalyzed by pig kidney trehalase. Carbohydr. Res., 194, 139-144 (1989).
33. Chiba, S., Molecular mechanism in α-glucosidase and glucoamylase. Biosci. Biotechnol. Biochem., 61, 1233-1239 (1997).
34. Someya, Y., Matsui, H., and Chiba, S., Chemical modification of histidyl residue in the active site of brewer's yeast α-glucosidase II. Agric. Biol. Chem., 48, 873-879 (1984).
35. Dixon, M. and Webb, E. C., Effect of pH, in "Enzymes," 3rd Ed., Academic Press, New York, pp. 138-164 (1979).