Primary structure and properties of the cathepsin G/chymotrypsin inhibitor from the larval hemolymph of Apis mellifera

European Journal of Biochemistry

Volumn 262, Issue 3, 1999, Pages 680-687

  Bania, Jacek ^b   Stachowiak, Damian ^b   Polanowski, Antoni ^a  

^a UNIVERSITY OF WROC AW   (Poland)

^b NONE

Author keywords

Ascaris inhibitor family; Cathepsin G inhibitor; Chymotrypsin inhibitor; Honey bee; Sequencing

Indexed keywords

CATHEPSIN G; CHYMOTRYPSIN; CHYMOTRYPSIN INHIBITOR; CYSTEINE;

AMINO ACID SEQUENCE; ARTICLE; ASCARIS; HEMOLYMPH; HONEYBEE; LARVAL DEVELOPMENT; NONHUMAN; PRIORITY JOURNAL; PROTEIN PURIFICATION; SEQUENCE HOMOLOGY;

AMINO ACID SEQUENCE; ANIMALS; BEES; BINDING SITES; BLOOD PROTEINS; CATHEPSINS; CHYMOTRYPSIN; HEAT; HEMOLYMPH; HONEY; HYDROLYSIS; INSECT PROTEINS; LARVA; MOLECULAR SEQUENCE DATA; PROTEASE INHIBITORS; PROTEIN DENATURATION; PROTEIN ISOFORMS; SEQUENCE ALIGNMENT; SERINE ENDOPEPTIDASES; THERMODYNAMICS;

EID: 0005945807     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1999.00406.x     Document Type: Article

References (27)

1. 1. Campbell, E.J., Silverman, E.K. & Campbell, M.A. (1989) Elastase and cathepsin G of human monocytes. Quantification of cellular content release in response to stimuli, and heterogeneity in elastase-mediated proteolytic activity. J. Immunol. 143, 2961-2968.
2. 2. Schechter, N.M., Wang, Z.M., Blacher, R.W., Lessin, S.R., Lazarus, O.S. & Rubin, H. (1994) Determination of the primery structure of human skin chymase and cathepsin G from cutaneous mast cells of urticaria pigmentosa lesions. J Immunol. 152, 4062-4069.
3. 3. Travis, J., Potempa, J., Bangalore, N. & Kurdowska, A. (1992) Multiple functions of neutrophil proteinases and their inhibitor complexes. In Biochemistry of Pulmonary Emphysema (Grassi, C., Travis, J., Casali, L. & Luisetti, M., eds), pp. 71-79. Springer-Verlag, London.
4. 4. Twinning, S.S. (1994) Regulation of proteolytic activity in tissues. CRC Crit. Rev. Biochem. Mol. Biol. 29, 315-383.
5. 5. Travis, J. (1988) Structure, function, and control of neutrophil proteinases. Am. J. Med. 84, 37-42.
6. 6. Polanowski, A., Wilusz, T., Blum, S.M., Escoubas, P., Schmidt, J.O. & Travis, J. (1992) Serine proteinase inhibitor profiles in the hemolymph of a wide range of insect species. Comp. Biochem. Physiol. 102B, 757-760.
7. 7. Watorek, W., Polanowski, A. & Wilusz, T. (1996) The use of sequential affinity chromatography for separation of human neutrophil elastase, cathepsin G and azurocidin. Acta Biochim. Polon. 234, 503-506.
8. 8. Otlewski, J., Polanowski, A., Leluk, J. & Wilusz, T. (1984) Trypsin inhibitors in summer squash (Cucurbita pepo) seeds. Isolation, purification and partial characterisation of three inhibitors. Acta Biochem. Polon. 31, 267-278.
9. 9. Bogard, W.C. Jr, Kato, I. & Laskowski, M. Jr (1980) A Ser162/Gly162 polymorphism in Japanese quail ovomucoid. J. Biol. Chem. 255, 6569-6574.
10. 10. Wolf, P. (1983) A critical reappraisal of Waddels technique for ultraviolet spectrophotometric protein estimation. Anal Biochem. 129, 145-155.
11. 11. Goldbarg, J.A. & Rutenburg, A.M. (1958) The colorimetric determination of leucine aminopeptidase in urine and serum of normal subjects and patients with cancer and other diseases. Cancer 11, 283-286.
12. 12. Chase, T. & Shaw, E. (1970) Titration of trypsin, plasmin, and thrombin with, p-nitrophenyl,p′-guanidinobenzoate HCl. Methods Enzymol. 19, 20-27.
13. 13. Empie, M.W. & Laskowski, M. Jr (1982) Thermodynamics and kinetics of single residue replacement in avian ovomucoid third domains: effect of inhibitor interactions with serine proteinases. Biochemistry 21, 2274-2284.
14. 14. Privalov, G., Kavina, V., Freire, E. & Privalov, P.L. (1995) Precise scaning calorimeter for studying thermal properties of biological macromolecules in dilute solutions. Anal. Biochem. 232, 79-85.
15. 15. Dyckers, D.E., Creighton, T.E. & Sheppard, R.C. (1978) [52-Homoserine]-basic pancreatic trypsin inhibitor. Preparation and properties of a protein analog. Int. J. Peptide Protein Res. 11, 258-268.
16. 16. Johnson, D. & Travis, J. (1979) The oxidative inactivation of human alpha-1 -proteinase inhibitor interactions with serine proteinases. J. Biol. Chem. 254, 4022-4026.
17. 17. Lavrence, D.A. & Loskutoff, D.J. (1986) Inactivation of plasminogen activator inhibitor by oxidants. Biochemistry 25, 6351-6355.
18. 18. Glazer, A.N., Delange, R.J. & Sigman, D.S. (1975) Chemical modification of proteins. In Selected Methods and Analytical Procedures, p. 103. North-Holland Publishing Company, Amsterdam.
19. 19. Leluk, J. (1997) A new algorithm for analysis of the homology in protein primary structure. Computers Chem. 22, 123-131.
20. 20. Makhatadze, G.I., Kim, K.-S., Woodward, C. & Privalov, P.L. (1993) Thermodynamics of BPTI folding. Protein Sci. 2, 2028-2036.
21. 21. Huang, K., Strynadka, N.C.J., Bernard, V.D., Peanasky, R.J. & James, M.N.G. (1994) The molecular structure of the complex of Ascaris chymotrypsin/elastase inhibitor with porcine elastase. Structure 2, 679-689.
22. 22. Betz, S.F. (1993) Disulfide bonds and the stability of globular proteins. Protein Sci. 2, 1551-1558.
23. 23. Babin, D.R., Peanasky, R.J. & Goss, S.M. (1984) The isoinhibitors of chymotrypsin/elastase from Ascaris lumbricoides; the primary structure. Arch. Biochem. Biophys. 232, 143-161.
24. 24. Verweij, C.L., Diergarde, P.J., Hart, M. & Pannekock, H. (1986) Full-length von Willebrand factor (vWF) cDNA encodes a highly repetitive protein cosiderably larger than the mature vWF subunit. EMBO J. 5, 1839-1847.
25. 25. Mignogna, G., Pascarella, S., Wechselberger, C., Hinterleitner, C., Mollay, C., Amiconi, G., Barra, D. & Kreil, G. (1996) BSTI, a trypsin inhibitor from skin secretions of Bambina bambina related to proteinase inhibitors of nematodes. Protein Sci. 5, 357-362.
26. 26. Bontems, F., Roumenstand, C., Gilquin, B., Menez, A. & Toma, F. (1991) Refined structure of charybolotoxin: common motifs in scorpion toxins and insect defensins. Science 254, 1521-1523.
27. 27. Palaghy, P.K., Nielsen, K.J., Craig, G.J. & Norton, R.S. (1994) A common structural motif incorporating a cystine knot and the triple stranded β-sheet in toxic and inhibitory polypeptides. Protein Sci. 3, 1833-1839.