Purification and characterization of a highly stable cysteine protease from the latex of ervatamia coronaria

Bioscience, Biotechnology and Biochemistry

Volumn 62, Issue 10, 1998, Pages 1947-1955

  Sundd, Monica ^a   Kundu, Suman ^a   Pal, Gour Pada ^a   Medicherla, Jagannadham V ^a  

^a BANARAS HINDU UNIVERSITY   (India)

Author keywords

Cysteine protease; Ervatamia coronaria; Ervatamin; Plant endopeptidase; Plant latex

Indexed keywords

CYSTEINE PROTEINASE; ERVATAMIN; LATEX;

AMINO ACID SEQUENCE; ARTICLE; CHEMISTRY; ENZYMOLOGY; ISOLATION AND PURIFICATION; MEDICINAL PLANT; METABOLISM; MOLECULAR GENETICS;

AMINO ACID SEQUENCE; CYSTEINE ENDOPEPTIDASES; LATEX; MOLECULAR SEQUENCE DATA; PLANTS, MEDICINAL;

EID: 0032177259     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.62.1947     Document Type: Article

References (30)

1. Ervatamia E. In “The Wealth Of India”, CSIR, New Delhi., Vol.3, pp. 192-193 (1952).
2. Asolkar, L. V., Kakkar, K. K., and Chakre, O. J., Ervatamia. In “Glossary of Indian medicinal plants with active principles”., Publications and Information Directorate, CSIR, New Delhi, Part I, pp. 298 (1992).
3. Gilman, A., Philips, F. S., Koelle, E. S., Allen, R. P., and John, St. E., The Metabolic reduction and nephrotoxic action of tetrathionate in relation to a possible interaction with sul-fhydryl compounds. Amer. J. Physiol., 147, 115-123 (1946).
4. Kimmel, J. R. and Smith, E. L., The properties of papain. Adv. Enzymol., 19, 267-334 (1957).
5. Sarath, G., Motte, R. S. de la., and Wagner, F. W., Protease assay methods. In “Proteolytic Enzymes-A Practical Approach”, eds. Beynon, R. J. and Bond, J. S., IRL Press, Oxford, pp. 25-55 (1989).
6. 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).
7. Arnon, R., Papain. Methods Enzymol., 19, 226-244 (1970).
8. Erlanger, B. F., Kokowsky, N., and Cohen, N., The preparation and properties of two new chromogenic infstrates of trypsin. Arch. Biochem. Biophys., 95, 271-278 (1961).
9. Segel, I. H., Enzymes. In “Biochemical Calculations” 2nd edition, John Wiley and Sons, USA, pp. 208-323 (1976).
10. Laemmli, U. K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-6855 (1970).
11. Shapira, E. and Arnon, R., Cleavage of one specific disulfide bond in papain. J. Biol. Chem., 244, 1026-1032 (1969).
12. Fish, W. W., Mann, K. G., and Tanford, C., The estimation of polypeptide chain molecular weights by gel filtration in 6 m guanidine hydrochloride. J. Biol. Chem., 244, 4989-4994 (1969).
13. Glazer, A. N. and Smith, E. L., Phenolic hydroxyl ionization in papain. J. Biol. Chem., 236, 2948-2951 (1961).
14. Aitken, A. and Learmonth, M., Protein determination by UV absorption. In “The Protein Protocols Handbook”, eds. Walker, J. M., Humana Press, Totowa, New Jersey, pp. 3-6 (1997).
15. Goodwin, W. and Morton, R. A., The spectrophotometric determination of tyrosine and tryptophan in proteins. Biochem. J., 40, 628-632 (1946).
16. Ellman, L., Tissue sulfhydryl groups. Arch. Biochem. Biophys., 82, 70-77 (1959).
17. Creighton, T. E., Disulfide bonds between protein residues. In “Protein Structure—A Practical Approach”, eds. Creighton, T. E., IRL Press, Oxford, pp. 155-160 (1989).
18. Riddles, P. W., Blakeley, R. L., and Zerner, B., Reassessment of Ellman’s reagent. Methods Enzymol., 91, 49-60 (1983).
19. Abraham, K. I. and Joshi, P. N., Studies on proteinases from Calotropis gigantea latex. I. Purification and some properties of two proteinases containing carbohydrate. Biochim. Biophys. Acta., 568, 111-119 (1979).
20. Takahashi, N., Yasuda, Y., Goto, K., Miyake, T., and Murachi, T., Multiple molecular forms of stem bromelain. Isolation and characterization of two closely related components, SB1 and SB2. J. Biochem., 74, 355-373 (1973).
21. Hounsell, E. F., Davies, M. J., and Smith, K. D., Chemical methods of analysis of glycoprotein. In “The Protein Protocols Handbook”, eds. Walker, J. M., Humana Press, Totowa, New Jersey, pp. 633-634 (1997).
22. Murachi, T., Bromelain enzymes. Methods Enzymol., 19, 273-285 (1970).
23. McDowall, M. A., Anionic proteinase from Actinidia chinensis. Preparation and properties of the crystalline enzyme. Eur. J. Biochem., 14, 214-221 (1970).
24. Ryan, C. A. and Walker-Simmons, M., Plant proteinases. In “The Biochemistry of Plants”, Vol. 6, Academic Press, New York, pp. 321-350 (1981).
25. Sumner, I. G., Harris, G. W., Taylor, M. A., Pickersgill, R. W., Owen, A. J., and Goodenough, P. W., Factors aifecting the thermostability of cysteine proteinases from Carica papaya. Eur. J. Biochem., 214, 129-234 (1993).
26. Mitchel, R. E., Chaiken, I. M., and Smith, E. L., The complete amino acid sequence of papain. Additions and corrections. J. Biol. Chem., 245, 3485-3492 (1970).
27. Lynn, K. R., Yaguchi, M., and Roy, C., Homologies of the N-terminal sequences of asclepains and papain. Biochim. Biophys. Acta., 624, 579-80 (1980).
28. Goto, K., Takahashi, N., and Murachi, T., Structural studies on stem bromelain. Cyanogen bromide cleavage and amino acid sequence of carboxyl terminal half of the molecule. Int. J. Pept. Protein Res., 15, 335-341 (1980).
29. Kaneda, M., Yonezawa, H., and Uchikoba, T., Purification and some properties of a protease from the sarcocarp of musk melon. Biosci. Biotechnol. Biochem., 61, 2100-2102 (1997).
30. Turk, B., Turk, V., and Turk, D., Structural and functional aspects of papain-like cysteine proteinases and their protein inhibitors. Biol. Chem., 378, 141-150 (1997).