Affinity purification and characterization of glucosidase II from pig liver

Biological Chemistry

Volumn 378, Issue 9, 1997, Pages 1031-1038

  Hentges, Andrea ^a   Bause, Ernst ^a  

^a UNIVERSITY OF BONN   (Germany)

Author keywords

Affinity purification; Glucosidase II from pig liver; Immunological cross reactivity; Inhibition by basic sugar analogues; Molecular and enzymic properties

Indexed keywords

1 DEOXYNOJIRIMYCIN; ASPARAGINE LINKED OLIGOSACCHARIDE; CARBOHYDRATE DERIVATIVE; CASTANOSPERMINE; CROSS REACTING ANTIBODY; ENZYME INHIBITOR; FLUORINE; GLUCOSIDASE; HYDROXYL GROUP; METAL ION; POLYCLONAL ANTIBODY; PROTEIN SUBUNIT; SEPHAROSE;

AFFINITY CHROMATOGRAPHY; AMINO ACID SEQUENCE; ANIMAL CELL; ANIMAL TISSUE; ARTICLE; CATTLE; CELL MEMBRANE; CELL STRAIN COS1; CELL TYPE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME BINDING; ENZYME GLYCOSYLATION; ENZYME INHIBITION; ENZYME INHIBITOR COMPLEX; ENZYME PURIFICATION; ENZYME SUBSTRATE COMPLEX; GENETIC CONSERVATION; HYDROLYSIS; IMMUNOBLOTTING; LIVER; LIVER MICROSOME; MOLECULAR WEIGHT; NONHUMAN; PH; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN PROCESSING; RAT; SWINE;

EID: 0030771750     PISSN: 14316730     EISSN: None     Source Type: Journal    
DOI: 10.1515/bchm.1997.378.9.1031     Document Type: Article

References (30)

1. Arakaki, R.F., Hedo, J.H., Collier, E., and Gordon, P. (1987). Effects of castanospermine and 1-deoxynojirimycin on insulin receptor biogenesis. J. Biol. Chem. 262, 11886-11892.
2. Bause, E., Günther, R., Schweden, J., and Tillmann, U. (1986). In vitro studies on the subcellular location of glucosidase I and glucosidase II in dog pancreas microsomes. Biosc. Reports 6, 827-834.
3. Bause, E., Schweden, J., Gross, A., and Orthen, B. (1989). Purification and characterization of trimming glucosidase I from pig liver. Eur. J. Biochem. 183, 661-669.
4. Brada, D., and Dubach, U.C. (1984). Isolation of homogeneous glucosidase II from pig kidney microsomes. Eur. J. Biochem. 141, 149-156.
5. Bray G.A. (1960). A simple efficient liquid scintillator for counting aqueous solutions in a liquid scintillation counter. Anal. Biochem. 1, 279-285.
6. Bramhall, S., Noack, N., Wu, M., and Loewenberg, J.R. (1969). A simple colorimetric method for determination of proteins. Anal. Biochem. 31, 146-156.
7. Breuer, W., and Bause, E. (1995). Oligosaccharyl transferase is a constitutive component of an oligomeric protein complex from pig liver endoplasmic reticulum. Eur. J. Biochem. 228, 689-696.
8. Burns, D.M., and Touster, O. (1982). Purification and characterization of glucosidase II, an endoplasmic reticulum hydrolase involved in glycoprotein biosynthesis. J. Biol. Chem. 257, 9991-10000.
9. Edwards, E.H., Sprague, E.A., Kelly, J.L., Kerbacher, J.J., Schwartz, C.J., and Elbein, A.D. (1989). Castanospermine inhibits the function of the low-density lipoprotein receptor. Biochemistry 28, 7679-7687.
10. Elbein, A.D. (1991). Glycosidase inhibitors: inhibitors of N-linked oligosaccharide processing. FASEB J. 5, 3055-3063.
11. Ganan, S., Cazzulo, J.J., and Parodi, J. (1991). A major proportion of N-glycoproteins are transiently glucosylated in the endoplasmic reticulum. Biochemistry 30, 3098-3104.
12. Helenius, A. (1994). How N-linked oligosaccharides affect glycoprotein folding in the endoplasmic reticulum. Mol. Biol. of the Cell 5, 253-265.
13. Henderson, L.E., Oroszlan, S., and Konigsberg, W. (1979). A micromethod for complete removal of dodecyl sulfate from proteins by ion-pair extraction. Anal. Biochem. 93, 153-157.
14. Hettkamp, H., Legler, G., and Bause, E. (1984). Purification by affinity chromatography of glucosidase I, an endoplasmic reticulum hydrolase involved in the processing of asparagine-linked oligosaccharides. Eur. J. Biochem. 142, 85-90.
15. Hino, Y., and Rothman, J.E. (1985). Glucosidase II, a glycoprotein of the endoplasmic reticulum membrane. Proteolytic cleavage into enzymatically active fragments. Biochemistry 24, 800-805.
16. Hoflack, B., Cacan, R., and Verbert, A. (1981). Dolichol pathway in lymphocytes from rat spleen. Influence of the glucosylation on the cleavage of dolichyl diphosphate oligosaccharides into phosphooligosaccharides. Eur. J. Biochem. 117, 285-290.
17. Kalz-Füller, B., Bieberich, E., and Bause, E. (1995). Cloning and expression of glucosidase I from human hippocampus. Eur. J. Biochem. 231, 344-351.
18. Kornfeld, R., and Kornfeld, S. (1985). Assembly of asparagine-linked oligosaccharides. Annu. Rev. Biochem. 54, 631-664.
19. Laemmli, U.K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 227, 680-685.
20. Legler, G. (1966). Untersuchungen zum Wirkungsmechanismus glykosidspaltender Enzyme: Darstellung und Eigenschaften spezifischer Inaktivatoren. Hoppe-Seyler's Z. Physiol. Chem. 345, 197-214.
21. Lowry, O.H., Rosebrough, N.J., Farr, A.L., and Randall, R.J. (1951). Protein measurement with the folin phenol reagent. J. Biol. Chem. 193, 265-275.
22. Lucocq, J.M., Brada, D., and Roth, J. (1986). Immunolocalization of the oligosaccharide trimming enzyme glucosidase II. J. Cell Biol. 102, 2137-2146.
23. Moore, S.E.H., and Spiro, R.G. (1993). Inhibition of glucose trimming by castanospermine results in rapid degradation of unassembled major histocompatibility complex class I molecules. J. Biol. Chem. 268, 3809-3812.
24. Moremen, K.W., Trimble, R.B., and Herscovics, A. (1994). Glycosidases of the asparagine-linked oligosaccharide processing pathway. Glycobiology 4, 113-125.
25. Saxena, S., Shailubhai, K., Dong-Yu, B., and Vijay, I.K. (1987). Purification and characterization of glucosidase II involved in N-linked glycoprotein processing in bovine mammary gland. Biochem. J. 247, 563-570.
26. 9-mannosidase from pig liver. Biochem. J. 264, 347-355.
27. 2-oligosaccharides. Eur. J. Biochem. 157, 563-570.
28. Sousa, M.C., Ferrero-Garcia, M.A., and Parodi, A.J. (1992). Recognition of the oligosaccharide and protein moieties of glycoproteins by the UDP-Glc-glycoprotein glucosyltransferase. Biochemistry 31, 97-105.
29. Spiro, R.G., Spiro, M.J., and Bhoyroo, V.D. (1979). Processing of carbohydrate units of glycoproteins. Characterization of a thyroid glucosidase. J. Biol. Chem. 254, 7659-7667.
30. Trombetta, E.S., Simons, J.F. and Helenius, A. (1996). Endoplasmic reticulum glucosidase II is composed of a catalytic subunit, conserved from yeast to mammals, and a tightly bound noncatalytic HDEL-containing subunit. J. Biol. Chem. 271, 27509-27516.