Partial purification and characterization of cysteine proteinase inhibitor from chicken plasma

Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology

Volumn 144, Issue 4, 2006, Pages 544-552

  Rawdkuen, Saroat ^a   Benjakul, Soottawat ^a   Visessanguan, Wonnop ^b   Lanier, Tyre C ^c  

^a PRINCE OF SONGKLA UNIVERSITY   (Thailand)

^b NATIONAL SCIENCE AND TECHNOLOGY DEVELOPMENT AGENCY   (Thailand)

^c NORTH CAROLINA STATE UNIVERSITY   (United States)

Author keywords

Autolysis; Chicken plasma; Cysteine proteinase inhibitor; Purification

Indexed keywords

CYSTEINE PROTEINASE INHIBITOR; MACROGOL; PAPAIN; SEPHAROSE; SODIUM CHLORIDE;

AFFINITY CHROMATOGRAPHY; ARTICLE; AUTOLYSIS; CHICKEN; DISULFIDE BOND; FRACTIONATION; HEATING; MOLECULAR WEIGHT; NONHUMAN; PLASMA; PRIORITY JOURNAL; PURIFICATION; STAINING;

GALLUS GALLUS; MERLANGIUS MERLANGUS; MERLUCCIUS PRODUCTUS; REINHARDTIUS STOMIAS;

EID: 33746494021     PISSN: 10964959     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbpb.2006.05.008     Document Type: Article

References (42)

1. Akpinar O., and An H. Purification and determination of inhibitory activity of recombinant soyacystatin for surimi application. Mol. Nutr. Food Res. 49 (2005) 247-255
2. An H., Weerasinghe V., Seymour T.A., and Morrissey M.T. Cathepsin degradation of Pacific whiting surimi protein. J. Food Sci. 59 (1994) 1013-1017
3. Anastasi A., Brown M.A., Kembhavi A.A., Nicklin M.J.H., Sayers C.A., Sunter D.C., and Barrett A.J. Cystatin, a protein inhibitor of cysteine proteinases. Biochem. J. 211 (1983) 129-138
4. Barrett A.J., Fritz H., Grubb A., Isemura S., Jarvinen M., Katunuma N., Machleidt W., Muller-Esterl W., Sasaki M., and Turk V. Nomenclature and classification of the proteins homologous with the cysteine-protease inhibitor chicken cystatin. Biochem. J. 236 (1986) 321
5. Benjakul S., and Visessanguan W. Pig plasma protein: potential use as proteinase inhibitor for surimi manufacture; inhibitory activity and the active components. J. Sci. Food Agric. 80 (2000) 1351-1356
6. Benjakul S., Seymour T.A., Morrissey M.T., and An H. Proteinase in Pacific whiting surimi wash water: identification and characterization. J. Food Sci. 61 (1996) 1165-1170
7. Benjakul S., Seymour T.A., Morrissey M.T., and An H. Characterization of proteinase from Pacific whiting surimi wash water. J. Food Biochem. 22 (1998) 1-16
8. Benjakul S., Visessanguan W., and Srivilai C. Porcine plasma protein as proteinase inhibitor in bigeye snapper (Priacanthus tayenus) muscle and surimi. J. Sci. Food Agric. 81 (2001) 1039-1046
9. Benjakul S., Visessanguan W., Ishizaki S., and Tanaka M. Differences in gelation characteristics of natural actomyosin from two species of bigeye snapper, Priacanthus tayenus and Priacanthus macracanthus. J. Food Sci. 66 (2001) 1311-1318
10. Brzin J., Popovic T., and Turk V. Human cystatin, a new protein inhibitor of cysteine proteinases. Biochem. Biophys. Res. Commun. 118 (1984) 103-109
11. Camargo Goncalvesa L.R., and Chudzinski-Tavassib A.M. High molecular mass kininogen inhibits metalloproteinases of Bothrops jararaca snake venom. Biochem. Biophys. Res. Commun. 318 (2004) 53-59
12. Garcia-Carreno F.L., Dimes L.E., and Haard N.F. Substrate-gel electrophoresis for composition and molecular weight of proteinases or proteinaceous proteinase inhibitors. Anal. Biochem. 214 (1993) 65-69
13. Gerhartz B., Engh R.A., Mentele R., Eckerskorn C., Torquato R., Wittmann J., Kolb H.J., Machleidt W., Fritz H., and Auerswald E.A. Quail cystatin: isolation and characterization of a new member of the cystatin family and its hypothetical interaction with cathepsin B. FEBS Lett. 412 (1997) 551-558
14. Hamann D.D., Amato P.M., Wu M.C., and Foegeding E.A. Inhibition of modori (gel weakening) in surimi by plasma hydrolysate and egg white. J. Food Sci. 55 (1990) 665-669
15. Hayashi I., Kato H., Iwanaga S., and Oh-ishi S. Rat plasma high-molecular weight kininogen. A simple method for purification and its characterization. J. Biol. Chem. 260 (1985) 6115-6123
16. Kimura M., Sueyoshi T., Takada K., Tanaka K., Morita T., and Iwanaga S. Isolation and characterization of ornitho-kininogen. Eur. J. Biochem. 168 (1988) 493-501
17. Komiya M., Kato H., and Suzuki T. Bovine plasma kininogens. Further purification of high molecular weight kininogen and its physicochemical properties. J. Biochem. 76 (1974) 811-822
18. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage. Nature 277 (1970) 680-685
19. Lee J.J., Tzeng S.S., and Jiang S.T. Purification and characterization of low molecular weight kininogen from pig plasma. J. Food Sci. 65 (2000) 81-86
20. Lowry O.H., Rosebrough N.J., Farr L.A., and Randall R.J. Protein measurement with the Folin phenol reagent. J. Biol. Chem. 193 (1951) 265-275
21. Mashiko H., and Takahashi H. Bullfrog plasma cysteine proteinase inhibitor (CPI). Immunopharmacology 32 (1996) 91-93
22. Mashiko H., and Takahashi H. Canine plasma kininogen: evidence for the presence of two kininogens and purification of high molecular weight kininogen and characterization as multi-functional molecule. Comp. Biochem. Physiol. B 117 (1997) 535-543
23. Mashiko H., Miyamoto K., and Takahashi H. Studies on porcine high molecular weight kininogen. An improved method for the purification of porcine high molecular weight kininogen and cleavage of the kininogen by the action of porcine plasma kallikrein. Comp. Biochem. Physiol. B 120 (1998) 647-656
24. Nakayasu T., and Nagasawa S. Studies on human kininogens: I. Isolation, characterization, and cleavage by plasma kallikrein of high molecular weight (HMW)-kininogen. J. Biochem. 85 (1979) 249-258
25. Rawdkuen S., Benjakul S., Visessanguan W., and Lanier T.C. Chicken plasma protein: proteinase inhibitory activity and its effect on surimi gel properties. Food Res. Int. 37 (2004) 156-165
26. Rawdkuen, S., Benjakul, S., Visessanguan, W., Lanier, T.C., in press. Cysteine proteinase inhibitor from chicken plasma: fractionation, characterization and its autolysis inhibition of myofibrillar proteins. Food Chem.
27. Record M.T.J., Zhang W., and Anderson C.F. Analysis of effects of salts and uncharged solutes on protein and nucleic acid equilibria and processes: a practical guide to recognizing and interpreting polyelectric effects, Hofmeister effects and osmotic effects of salts. Adv. Protein Chem. 51 (1998) 281-353
28. Richard K., Owusu A., and Kritika M. The heat resistance and conformational plasticity of Kunitz soybean trypsin inhibitor. J. Food Biochem. 23 (1999) 209-224
29. Robinson H.W., and Hodgen C.G. The biuret reaction in the determination of serum protein: I. A study of the condition necessary for the production of the stable color which bears a quantitative relationship to the protein concentration. J. Biol. Chem. 135 (1940) 707-725
30. Sadaf Z., and Bilqees S.B. Isolation, characterization and kinetics of goat cystatins. Comp. Biochem. Physiol. B 142 (2005) 361-368
31. Saito A., and Kitano Y. Comparative studies on the cysteine proteinase inhibitory capacity of mammalian blood. Tohoku J. Exp. Med. 190 (2000) 83-92
32. Semba U., Shibuya Y., Okabe1 H., Hayashi I., and Yamamoto T. Whale high-molecular-weight and low-molecular-weight kininogens. Thromb. Res. 97 (2000) 481-490
33. Semba U., Umeda Y., Shibuya Y., Okabe H., Tanase S., and Yamamoto T. Primary structures of guinea pig high- and low-molecular weight kininogens. Int. Immunopharmacol. 4 (2004) 1391-1400
34. Sugo T., Kato H., Iwanaga S., and Fujii S. Occurrence of Leu-Lys-bradykinin and histidine-rich peptide in high-molecular weight kininogen isolated from horse plasma. Biochim. Biophys. Acta 579 (1979) 474-478
35. Timashaff S.N., and Arakawa T. Protein Structure: A Practical Approach (1997), IRL Press, Oxford
36. Turk V., and Bode W. The cystatins: protein inhibitors of cysteine proteinases. FEBS Lett. 285 (1991) 213-219
37. Turk B., Turk V., and Salvesen G.S. Regulating cysteine protease activity: essential role of protease inhibitors as guardians and regulators. Curr. Pharm. Des. 8 (2002) 1623-1637
38. Visessanguan W., and An H. Effects of proteolysis and mechanism of gel weakening in heat-induced gelation of fish myosin. J. Agric. Food Chem. 48 (2000) 1024-1032
39. Visessanguan W., Benjakul S., and An H. Purification and characterization of cathepsin L in arrowtooth flounder (Atheresthes stomias) muscle. Comp. Biochem. Physiol. B 134 (2003) 477-487
40. Wasson D.H., Reppond K.D., Babbitt J.K., and French J.S. Effect of additives on proteolytic and functional properties of arrowtooth flounder surimi. J. Aquat. Food Prod. Technol. 1 (1992) 147-165
41. Yamamoto T. Characterization of guinea pig high-molecular weight kininogen as multi-functional molecule. Biochim. Biophys. Acta 914 (1987) 259-274
42. Yoshida K., Saito A., and Sinohara H. Isolation and partial characterization of a novel form of low molecular weight kininogen from guinea pig plasma. Biochem. Int. 19 (1989) 1339-1344