Ostrich intestinal glycohydrolases: Distribution, purification and partial characterisation

International Journal of Biochemistry and Cell Biology

Volumn 30, Issue 3, 1998, Pages 339-352

  Oosthuizen, Vaughan ^a   Weldrick, Durand P ^a   Naudé, Ryno J ^a   Oelofsen, Willem ^a   Muramoto, Koji ^b   Kamiya, Hisao ^b  

^a NELSON MANDELA METROPOLITAN UNIVERSITY   (South Africa)

^b KITASATO UNIVERSITY   (Japan)

Author keywords

Intestinal glycohydrolases; Kinetics; Ostrich; Purification

Indexed keywords

ALPHA GLUCOSIDASE; GLYCOGEN; GLYCOSIDASE; ISOMALTOSE; LACTASE; MALTOSE; MALTOTRIOSE; OLIGOSACCHARIDE; SEPHADEX; STARCH; SUCRASE ISOMALTASE; SUCROSE; TETROSE; TREHALASE;

AFFINITY CHROMATOGRAPHY; AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ANIMAL TISSUE; ARTICLE; BIRD; BRUSH BORDER; CARBOHYDRATE METABOLISM; CHEMICAL REACTION KINETICS; ENZYME ACTIVITY; ENZYME INHIBITION; ENZYME LOCALIZATION; ENZYME PURIFICATION; ENZYME STRUCTURE; ENZYME SUBUNIT; GEL FILTRATION CHROMATOGRAPHY; NONHUMAN; SEQUENCE HOMOLOGY;

AMINO ACID SEQUENCE; AMINO ACIDS; ANIMALS; BIRDS; GLUCAN 1,4-ALPHA-GLUCOSIDASE; GLYCOSIDE HYDROLASES; HUMANS; HYDROGEN-ION CONCENTRATION; INTESTINES; KINETICS; MICROVILLI; MOLECULAR SEQUENCE DATA; MOLECULAR WEIGHT; SEQUENCE HOMOLOGY, AMINO ACID; SPECIES SPECIFICITY; SUCRASE-ISOMALTASE COMPLEX; SWINE; TISSUE DISTRIBUTION;

ANIMALIA; AVES; FELIS CATUS; STRUTHIO CAMELUS; SUIDAE;

EID: 0031803255     PISSN: 13572725     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1357-2725(97)00126-X     Document Type: Article

References (46)

1. Van Beers E.H., Büller H.A., Grand R.J., Einerhand A.W.C., Dekker J. Intestinal brush border glycohydrolases: Structure, function and development. Crit. Rev. Biochem. Mol. Biol. 30:1995;197-262.
2. Zhu J.S., Conklin K.A., Scheving L.A., Smith A.J., Gray G.M. Structural and functional correlates of sucrase-α-dextrinase in intact brush border membranes. Biochemistry. 30:1991;10399-10408.
3. Naim H.Y., Sterchi E.E., Lentze M.J. Biosynthesis of the human sucrase-isomaltase complex. Differential O-glycosylation of the sucrase subunit correlates with its position within the enzyme complex. J. Biol. Chem. 263:1988;7242-7253.
4. Hu C.-B., Spiess M., Semenza G. The mode of anchoring and precursor forms of sucrase-isomaltase and maltase-glucoamylase in chicken intestinal brush border membrane. Phylogenetic implications. Biochim. Biophys. Acta. 896:1987;275-286.
5. Semenza G., Auricchio S., Rubino A. Multiplicity of human intestinal disaccharidases. I Chromatographic separation of maltases and of two lactases. Biochim. Biophys. Acta. 96:1965;487-497.
6. Gray G.M., Lally B.C., Conklin K.A. Action of intestinal sucrase-isomaltase and its free monomers on an α-limit dextrin. J. Biol. Chem. 254:1979;6038-6043.
7. Sørensen S.H., Norén O., Sjöström H., Danielsen E.M. Amphiphilic pig intestinal microvillus maltase-glucoamylase. Structure and specificity. Eur. J. Biochem. 126:1982;559-568.
8. Taravel F.R., Datema R., Woloszczuk W., Marshall J.J., Whelan W.J. Purification and characterisation of a pig intestinal α-limit dextrinase. Eur. J. Biochem. 130:1983;147-153.
9. Hunziker W., Spiess M., Semenza G., Lodish H.F. The sucrase-isomaltase complex: Primary structure, membrane orientation, and evolution of a stalked, intrinsic brush border protein. Cell. 46:1986;227-234.
10. Chantret I., Lacasa M., Chevalier G., Ruf J., Islam I., Mantei N., Edwards Y., Swallow D., Rousset M. Sequence of the complete cDNA and the 5′ structure of the human sucrase-isomaltase gene. Biochem. J. 285:1992;915-923.
11. Chandrasena G., Osterholm D.E., Sunitha I., Henning S.J. Cloning and sequencing of a full-length rat sucrase-isomaltase-encoding cDNA. Gene. 150:1994;355-360.
12. G. Semenza, The mode of anchoring of sucrase-isomaltase to the small intestinal brush-border membrane and its biosynthetic implications, in: S. Rapoport, T. Schewe (Eds.), Proc. 12th FEBS Meeting, Dresden, Vol 53, Pergamon Press, Oxford, New York, 1978, pp. 21-28.
13. Prakash K., Patil S.D., Hedge S.N. Studies on the intestinal disaccharidases of the pigeon. III Separation, purification and properties of sucrase-isomaltase and maltase-glucoamylase. Arch. Int. Physiol. Biochim. 91:1983;379-390.
14. Vasseur M. Purification of the rabbit small intestinal sucrase-isomaltase complex: Separation from other maltases. Biosci. Rep. 9:1989;341-346.
15. Koldovsky O., Asp N.G., Dahlqvist A. A method for the separate assay of 'neutral' and 'acid' β-galactosidase in homogenates of rat small-intestinal mucosa. Anal. Biochem. 27:1969;409-418.
16. Schlegel-Haueter S., Hore P., Kerry K.R., Semenza G. The preparation of lactase and glucoamylase of rat small intestine. Biochim. Biophys. Acta. 258:1972;506-519.
17. Kessler M., Acuto O., Storelli C., Murer H., Müller M., Semenza G. A modified procedure for the rapid preparation of efficiently transporting vesicles from small intestinal brush border membranes. Their use in investigating some properties of D-glucose and choline transport systems. Biochim. Biophys. Acta. 506:1978;136-154.
18. Tsuboi K.K., Schwartz S.M., Burrill P.H., Kwong L.K., Sunshine P. Sugar hydrolases of the infant rat intestine and their arrangement on the brush border membrane. Biochim. Biophys. Acta. 554:1979;234-248.
19. Lowry O.H., Rosebrough N.J., Farr A.L., Randall R.J. Protein measurement with the Folin phenol reagent. J. Biol. Chem. 193:1951;265-275.
20. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of a bacteriophage T4. Nature. 227:1970;680-685.
21. Dunbar B.S., Kimura H., Timmons T.M. Protein analysis using high-resolution two-dimensional polyacrylamide gel electrophoresis. Methods Enzymol. 182:1990;441-459.
22. Robertson E., Danley H., Malloy P., Reeves H. Rapid isoelectric focusing in a vertical polyacrylamide minigel system. Anal. Biochem. 167:1987;290-294.
23. Mukasa H., Shimamura A., Tsumori H. Direct activity stains for glycosidases and glucosyltransferase after isoelectric focusing in horizontal polyacrylamide gel layers. Anal. Biochem. 123:1982;276-284.
24. Matsudaira P. Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes. J. Biol. Chem. 262:1987;10035-10038.
25. Knecht R., Chang J. Liquid chromatographic determination of amino acids after gas-phase hydrolysis and derivatisation with (dimethylamino)azobenzenesulphonyl chloride. Anal. Chem. 58:1986;2375-2379.
26. K. Muramoto, K. Nokihara, A. Ueda, H. Kamiya, Sensitisation of gas-phase protein sequencer using fluorescein isothiocyanate (FITC), in: K. Imahori, F. Sakiyama (Ed.s), Methods in Protein Sequence Analysis, Plenum Press, New York, 1993, pp. 29-36.
27. Hanes C.S. Studies on plant amylases. The effect of starch concentration upon the velocity of hydrolysis by the amylase of germinated barley. Biochem. J. 26:1932;1406-1411.
28. Triadou N., Bataille J., Schmitz J. Longitudinal study of the human intestinal brush border membrane proteins. Distribution of the main disaccharidases and peptidases. Gastroenterol. 85:1983;1326-1332.
29. Siddons R.C. Intestinal disaccharidase activities in the chick. Biochem. J. 112:1969;51-59.
30. Takesue Y., Kashiwagi T. Solubilisation and behaviour toward Sephadex of rabbit intestinal sucrase. J. Biochem. 65:1969;427-434.
31. Lee L., Forstner G. Rat intestinal maltase-glucoamylase. Purification of the detergent-solubilised enzyme in the presence of protease inhibitors: Properties and identification of a protease-sensitive subunit. Can. J. Biochem. Cell Biol. 62:1984;26-43.
32. Norén O., Sjöström H., Cowell G.M., Tranum-Jensen J., Hansen O.C., Welinder K.G. Pig intestinal microvillar maltase-glucoamylase. Structure and membrane insertion. J. Biol. Chem. 261:1986;12306-12309.
33. Quaroni A., Gershon-Quaroni E., Semenza G. Tryptic digestion of native small intestinal sucrase-isomaltase complex: Isolation of the sucrase subunit. Eur. J. Biochem. 52:1975;481-486.
34. Heymann H., Günther G. Calculation of subsite affinities of small intestinal glucoamylase-maltase. Biol. Chem. Hoppe-Seyler. 375:1994;451-455.
35. Sivakami S., Radhakrisnan A.N. A comparative study of maltase and glucoamylase in the intestine of various animal species. Ind. J. Exp. Biol. 13:1975;238-241.
36. Sell J.L., Koldovsky O., Reid B.L. Intestinal disaccharidases of young turkeys: Temporal development and influence of diet composition. Poultr. Sci. 68:1989;265-277.
37. Sir El Khatim M.M., Osman A.M. The level and distribution of disaccharidases in the camel (Camelus dromedarius) intestine. Comp. Biochem. Physiol. 71A:1982;199-204.
38. Martínez del Rio C., Stevens B.R. Intestinal brush border membrane bound disaccharidases of the American alligator. Alligator mississippiensis. Comp. Biochem. Physiol. 91B:1988;751-754.
39. Kolínská J., Kraml J. Separation and characterisation of sucrase-isomaltase and of glucoamylase of rat intestine. Biochim. Biophys. Acta. 284:1972;235-247.
40. Cowell G.M., Tranum-Jensen J., Sjöström H., Norén O. Topology and quaternary structure of pro-sucrase/isomaltase and final-form sucrase/isomaltase. Biochem. J. 237:1986;455-461.
41. 2+-precipitated enterocyte membranes. FEBS Lett. 127:1981;129-132.
42. Hauri H.-P., Sterchi E.E., Bienz D., Fransen J.A.M., Marxer A. Expression and intracellular transport of microvillus membrane hydrolases in human intestine. J. Cell Biol. 101:1985;838-851.
43. Hoffman L.R., Chang E.B. Determinants of regional sucrase-isomaltase expression in adult rat small intestine. J. Biol. Chem. 266:1991;21815-21820.
44. Naim H.Y., Roth J., Sterchi E.E., Lentze M., Milia P., Schmitz J., Hauri H.-P. Sucrase-isomaltase deficiency in humans. Different mutations disrupt intracellular transport, processing and function of an intestinal brush border enzyme. J. Clin. Invest. 82:1988;667-679.
45. Hauri H.-P., Quaroni A., Isselbacher K.J. Biogenesis of intestinal plasma membrane: Posttranslational route and cleavage of sucrase-isomaltase. Proc. Natl. Acad. Sci. USA. 76:1979;5183-5186.
46. Danielsen E.M., Sjöström H., Norén O. Biosynthesis of intestinal microvillar proteins. Pulse-chase labelling studies on maltase-glucoamylase, aminopeptidase A and dipeptidyl peptidase IV. Biochem. J. 210:1983;389-393.