Purification of a multicatalytic protease complex from developing winged bean seeds by indirect immunoaffinity chromatography

Protein Expression and Purification

Volumn 15, Issue 1, 1999, Pages 48-56

  Usha, Rajamma ^a   Singh, Manoranjan ^a  

^a INDIAN INSTITUTE OF CHEMICAL BIOLOGY   (India)

Author keywords

[No Author keywords available]

Indexed keywords

CHYMOTRYPSIN INHIBITOR; ENZYME INHIBITOR; ENZYME PURIFICATION; GEL PERMEATION CHROMATOGRAPHY; IMMUNOAFFINITY CHROMATOGRAPHY; PROTEINASE; SDS POLYACRYLAMIDE GEL ELECTROPHORESIS;

GLYCINE MAX; PHASEOLUS (ANGIOSPERM); PSOPHOCARPUS TETRAGONOLOBUS; TETRAGONOLOBUS;

EID: 0033083534     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1006/prep.1998.0982     Document Type: Article

References (38)

1. Ryan C. A. Proteinase inhibitors. The Biochemistry of Plants: A Comprehensive Treatise. 1981;Academic Press, New York. p. 351-370.
2. Richardson M. The proteinase inhibitors of plant and microorganism. Phytochemistry. 16:1977;159-169.
3. Ryan C. A. Protease inhibitors in plants: Genes for improving defenses against insects and pathogens. Annu. Rev. Phytopathol. 28:1990;425-449.
4. Johnson R., Narvaez J., An G., Ryan C. A. Expression of protease inhibitors I and II in transgenic tobacco plants: Effects on natural defense againstManduca sexta. Proc. Natl. Acad. Sci. USA. 86:1989;9871-9875.
5. Laskowski M., Kato I. Protein inhibitors of proteinases. Annu. Rev. Biochem. 49:1980;593-626.
6. Baudyš M., Ghosh M., Harlos K., Mareš M., Fusek M., Kostka V., Blake C. Crystallization and preliminary crystallographic study of cathepsin D inhibitor from potatoes. J. Mol. Biol. 218:1991;21-22.
7. Abe M., Arai S., Kato H., Fujimaki M. Thiol-protease inhibitors occuring in endosperm of corn. Agric. Biol. Chem. 44:1980;685-686.
8. Nishikata M. Trypsin-like protease from soybean seeds: Purification and some properties. J. Biochem. 95:1984;1169-1177.
9. Morita S., Fukase M., Hoshino K., Fukuda Y., Yamaguchi M., Morita Y. Partial purification and characterization of a novel soybean protease which is inhibited by Kunitz and Bowman-Birk trypsin inhibitors. J. Biochem. 119:1996;711-718.
10. Kortt A. A. Isolation and characterization of the trypsin inhibitors from winged bean seed (Psophocarpus tetragonolobus. Biochim. Biophys. Acta. 577:1979;371-382.
11. Roy A., Singh M. Purification of a storage protein ofPsophocarpus tetragonolobus. Phytochemistry. 26:1986;595-600.
12. 1Psophocarpus tetragonolobus, Phytochemistry. 27:1988;31-34.
13. Duttagupta J. K., Podder A., Chakrabarti C., Sen U., Dutta S. K., Singh M. Structure of a Kunitz-type chymotrypsin inhibitor from winged bean seeds at 2.95 Å resolution. Acta. Crystallogr. D52:1996;521-528.
14. Shibata H., Hara S., Ikenaka T., Abe J. Purification and characterization of proteinase inhibitors from winged bean (Psophocarpus tetragonolobus. J. Biochem. 99:1986;1147-1155.
15. Habu Y., Peyachoknagul S., Sakata Y., Fukasawa K., Ohno T. Evolution of a multigene family that encodes the Kunitz chymotrypsin inhibitor in winged bean: A possible intermediate in the generation of a new gene with a distinct pattern of expression. Mol. Gen. Genet. 254:1997;73-80.
16. Ghosh S., Singh M. cDNA cloning, expression and rapid purification of a Kunitz-type winged bean chymotrypsin inhibitor. Protein Express. Purif. 10:1997;100-106.
17. Baumeister W., Walz J., Zuhl F., Seemuller E. The proteasome: Paradigm of a self-compartmentalizing protease. Cell. 92:1998;367-380.
18. Orlowski M., Wilk S. A multicatalytic protease complex from pituitary that forms enkephalin and enkephalin containing peptides. Biochem. Biophys. Res. Commun. 101:1981;814-822.
19. Hochstrasser M. Ubiquitin, proteasomes and the regulation of intracellular protein degradation. Curr. Opin. Cell Biol. 7:1995;215-223.
20. Tamura T., Nagy I., Lupas A., Lottspeich F., Cejka Z., Schoofs G., Tanaka K., De Mot R., Baumeister W. The first characterization of a eubacterial proteasome: The 20 S complex of Rhodococcus. Curr. Biol. 5:1995;766-774.
21. Ozaki M., Fujinami K., Tanaka K., Amemiya Y., Sato T., Ogura N., Nakagawa H. Purification and characterization of the proteasome from the higher plantSpinacia oleracea. J. Biol. Chem. 267:1992;21678-21684.
22. Tanaka K., Tsurumi C. The 26S proteasome: Subunits and functions. Mol. Biol. Rep. 24:1997;3-11.
23. Fujinami K., Tanahashi N., Tanaka K., Ichihara A., Cejka Z., Baumeister W., Miyawaki M., Sato T., Nakagawa H. Purification and characterization of the 26 S proteasome from spinach leaves. J. Biol. Chem. 269:1994;25905-25910.
24. Vierstra R. D. Proteolysis in plants: Mechanisms and functions. Plant Mol. Biol. 32:1996;275-302.
25. Umeda M., Fujii N., Manabe Y., Uchimiya H. Molecular and biochemical characterization of a proteasome subunit from rice and carrot cells. Mol. Gen. Genet. 255:1997;19-27.
26. Murakami Y., Matsufuji S., Kameji T., Hayashi S., Igarashi S., Igarashi K., Tamura T., Tanaka K., Ichihara A. Ornithine decarboxylase is degraded by the 26 S proteasome without ubiquitination. Nature. 360:1992;597-599.
27. Jentoft N., Dearborn D. G. Labeling of proteins by reductive methylation using sodium cyanoborohydride. J. Biol. Chem. 254:1979;4359-4365.
28. Erlich H. A., Cohen S. N., McDevitt H. O. Immunological detection and characterization of products translated from cloned DNA fragments. Methods Enzymol. 68:1979;443-453.
29. Wilchek M., Miron T., Kohn J. Affinity chromatography. Methods Enzymol. 104:1984;3-55.
30. Usha R., Singh M. Proteases of germinating winged-bean seeds: Purification and partial characterization of an acidic protease. Biochem. J. 313:1996;423-429.
31. Heussen C., Dowdle E. B. Electrophoretic analysis of plasminogen activators in polyacrylamide gels containing sodium dodecyl sulfate and copolymerized substrates. Anal. Biochem. 102:1980;196-202.
32. Tanaka K., Yoshimura T., Kumztori A., Ichihara A., Ikai A., Nishigai M., Kameyama K., Takagi T. Proteasomes (multi-protease complex) as 20 S ring shaped particles in a variety of eukaryotic cells. J. Biol. Chem. 263:1988;16209-16217.
33. 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. 72:1976;248-254.
34. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
35. Towbin H., Staehlin T., Gordon J. Electrophoretic transfer from polyacrylamide gels to nitrocellulose sheets: Procedures and some applications. Proc. Natl. Acad. Sci. USA. 76:1979;4350-4354.
36. Arrigo A. R., Simon M., Darlix J. L., Spahr P. F. A 20 S particle ubiquitous from yeast to man. J. Mol. Evol. 25:1987;141-150.
37. Northwang H. G., Coux O., Bey F., Scherrer K. Prosomes and their multicatalytic proteinase activity. Eur. J. Biochem. 207:1992;621-630.
38. Tanaka K., Yoshimura T., Ichihara A. Role of substrate in reversible activation of proteasomes (multi-protease complexes) by sodium dodecyl sulfate. J. Biochem. 106:1989;495-500.