Isolation and amino-acid sequence of two inhibitors of serine proteinases, members of the squash inhibitor family, from Echinocystis lobata seeds

Acta Biochimica Polonica

Volumn 43, Issue 3, 1996, Pages 507-514

  Stachowiak, Damian ^a   Polanowski, Antoni ^a   Bieniarz, Grazyna ^a   Wilusz, Tadeusz ^a  

^a UNIVERSITY OF WROC AW   (Poland)

Author keywords

Amino acid sequence; Cathepsin G inhibitor; Cucubitaceae; Echinocystis lobata; Squash inhibitor family; Trypsin inhibitor

Indexed keywords

BOVINAE; ECHINOCYSTIS LOBATA; LOBATA;

SERINE PROTEINASE INHIBITOR;

AFFINITY CHROMATOGRAPHY; AMINO ACID SEQUENCE; ARTICLE; CHEMISTRY; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; ION EXCHANGE CHROMATOGRAPHY; ISOLATION AND PURIFICATION; MOLECULAR GENETICS; VEGETABLE;

AMINO ACID SEQUENCE; CHROMATOGRAPHY, AFFINITY; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; CHROMATOGRAPHY, ION EXCHANGE; MOLECULAR SEQUENCE DATA; SERINE PROTEINASE INHIBITORS; VEGETABLES;

EID: 0030331080     PISSN: 0001527X     EISSN: None     Source Type: Journal    
DOI: 10.18388/abp.1996_4484     Document Type: Article

References (32)

1. Polanowski, A., Wilusz, T., Nienartowicz, B., Cieślar, E., Słomińska, E. & Nowak, K. (1980) Isolation and partial amino acid sequence of the trypsin inhibitor from the seeds of Cucurbita maxima. Acta Biochim. Polon. 27, 371-382.
2. Wieczorek, M., Otlewski, J., Cook, J., Parks, K., Leluk, J., Wilimowska-Pelc, A., Polanowski, A., Wilusz, T. & Laskowski, M., Jr. (1985) The squash family of serine proteinase inhibitors. Amino acid sequences and association equilibrium constants of inhibitors from squash, summer squash, zucchini, and cucumber seeds. Biochem. Biophys. Res. Commun. 126, 646-652.
3. Otlewski, J., Whatley, H., Polanowski, A. & Wilusz, T. (1987) Amino-acid sequences of trypsin inhibitors from watermelon (Citrulus vulgaris) and red bryony (Bryonia dioica) seeds. Biol. Chem. Happe-Seyler 368, 1505-1507.
4. Joubert, F.J. (1984) Trypsin isoinhibitors from Momordica repens seeds. Phytochemistry 23, 1401-1406.
5. 1H 2D NMR and distance geometry study of the folding of Ecballium elaterium trypsin inhibitor, a member of the squash inhibitors family. Biochemistry 28, 2392-2398.
6. Nishino, J., Takano, R., Kamei-Hayashi, K., Minakata, H., Nomoto, K. & Hara, S. (1992) Amino acid sequences of trypsin inhibitors from oriental pickling melon (Cucumis melo L. var. Conomon Makino) seeds. Biosci. Biotech. Biochem. 56, 1241-1246.
7. Lee, Ch.-F. & Lin, J.-Y. (1995) Amino acid sequences of trypsin inhibitors from the melon Cucumis melo. J. Biochem. 118, 18-22.
8. Hatakeyama, T., Hiraoka, M. & Funatsu, G., (1991) Amino acid sequences of the two smallest trypsin inhibitors from sponge gourd seeds. Agric. Biol. Chem. 55, 2641-2642.
9. Ling, M.-H., Qi, H.-Y. & Chi, Ch.-W. (1993) Protein, cDNA, and genomic DNA sequences of the towel gourd trypsin inhibitor, a squash family inhibitor. J. Biol. Chem. 268, 810-814.
10. Matsuo, M., Hamato, N., Takano, R., Kamei-Hayashi, K., Yasuda-Kamatani, Y., Nomoto, K. & Hara, S. (1992) Trypsin inhibitors from bottle - gourd (Lagenaria leucantha Rusby var. Depressa Makino) seeds. Purification and amino acid sequences. Biochim. Biophys. Acta. 1120, 187-192.
11. Hayashi, K., Takehisa, T., Hamato, N., Takano, R., Hara, S., Miyata, T. & Kato, H. (1994) Inhibition of serine proteinases of the blood coagulation system by squash family proteinase inhibitors. J. Biochem. (Tokyo) 116, 1013-1018.
12. Hamato, N., Koshiba, T., Pham, T.-N., Tatsumi, Y., Nakamura, D., Takano, R., Hayashi, K., Hong, Y.-M. & Hara, S. (1995) Trypsin and elastase inhibitors from bitter gourd (Momordica charantia Linn.) seeds. Purification, amino acid sequences, and inhibitory activity of four new inhibitors. J. Biochem. (Tokyo) 117, 432-437.
13. Haldar, U.C., Saha, S.K., Beavis, R.C. & Sinha, N.K. (1996) Trypsin inhibitors from ridged gourd (Luffa acutangula Linn) seeds: Purification, properties, and amino acid sequences. J. Protein Chem. 15, 177-184.
14. Huang, Q., Liu, H. & Tang, Y. (1993) Refined 1.6 Å resolution crystal structure of the complex formed between porcine β-trypsin and CMTI-A, a trypsin inhibitor of the squash family. Detailed comparison with bovine β-trypsin and its complex. J. Mol. Biol. 229, 1022-1036.
15. Bode, W., Greyling, H.J., Huber, R., Otlewski, J. & Wilusz, T. (1989) The refined 2.0 Å X-ray crystal structure of the complex formed between bovine β-trypsin and CMTI-I, a trypsin inhibitor from squash seeds (Cucurbita maxima). Topological similarity of the squash seed inhibitors with the carboxypeptidase A inhibitor from potatoes. FEBS Lett. 242, 285-292.
16. 1H-n.m.r. studies of squash seed trypsin inhibitor. Int. J. Peptide Protein Res. 43, 381-386.
17. Holak, T.A., Gondol, D., Otlewski, J. & Wilusz, T. (1989) Determination of the complete three-dimensional structure of the trypsin inhibitor from squash seeds in aqueous solution by nuclear magnetic resonance and a combination of distance geometry and dynamical simulated annealing. J. Mol. Biol. 210, 635-648.
18. Krishnamoorthi, R. & Sun Lin Ch.-L. (1992) Structural consequences of the natural substitution, E9K, on reactive-site-hydrolyzed squash (Cucurbita maxima) trypsin inhibitor (CMTI) as studied by two-dimensional NMR. Biochemistry 31, 4965-4969.
19. Chen, X.-M., Qian, Y.-W., Chi, Ch.-W., Gan, K.-D., Zhang, M.-F. & Chen, Ch.-Q. (1992) Chemical synthesis, molecular cloning and expression of the gene coding for the Trichosanthes trypsin inhibitor - a squash family inhibitor. J. Biochem. (Tokyo) 112, 45-51.
20. Rolka, K., Kupryszewski, G., Ragnarsson, U., Otlewski, J., Krokoszyńska, I. & Wilusz, T. (1991) Chemical synthesis of new trypsin, chymotrypsin and elastase inhibitors by amino-acid substitution in a trypsin inhibitor from squash seeds (CMTI III) Biol. Chem. Hoppe-Seyler 372, 63-68.
21. Bolewska, K., Krowarsch, D., Otlewski, J., Jaroszewski, Ł. & Bierzyński, A. (1995) Synthesis, cloning and expression in Escherichia coli of a gene coding for the Met⇒Leu CMTI I - a representative of the squash inhibitors of serine proteinases. FEBS Lett. 377, 172-174.
22. Rempoła, B., Wilusz, T., Markiewicz, W. & Fikus, M. (1995) Synthesis, cloning and expression in Escherichia coli of the gene coding for the trypsin inhibitor from Cucurbita pepo. Acta Biochim. Polon. 42, 109-114.
23. Wilimowska-Pelc, A. & Mejbaum-Katzenellenbogen, W. (1978) A simple method for isolating trypsin from trichloroacetic acid extracts of bovine pancreas. Anal. Biochem. 90, 816-820.
24. Liepniecks, J.J. & Light, A. (1974) Preparation of β-trypsin by affinity chromatography of enterokinase-activated bovine trypsinogen. Anal. Biochem. 60, 395-404.
25. Ako, H., Foster, R.J. & Ryan, C.A. (1972) The preparation of anhydro-trypsin and its reactivity with naturally occurring proteinase inhibitors. Biochem. Biophys. Res. Commun. 47, 1402-1407.
26. Chase, T. & Shaw, E. (1970) Titration of trypsin, plasmin and thrombin with p-nitrophenyl p'-guanidinobenzoate HCl. Methods Enzymol. 19, 20-27.
27. Erlanger, B.F., Kokowsky, N. & Cohen, W. (1961) The preparation and properties of two new chromogenic substrates of trypsin. Arch. Biochem. Biophys. 95, 271-278.
28. Wa̧torek, W., Polanowski, A. & Wilusz, T. (1996) The use of sequencial affinity chromatography for separation of human neutrophil elastase, cathepsin G and azurocidin. Acta Biochim. Polon. 43, 503-506.
29. Empie, M. & Laskowski, M., Jr. (1982) Thermodynamics and kinetics of single residue replacements in avian ovomucoid third domains: effect on inhibitor interactions with serine proteinases. Biochemistry 21, 2274-2284.
30. Otlewski, J., Zbyryt, T., Krokoszyńska, I. & Wilusz, T. (1990) Inhibition of serine proteinases by squash inhibitors. Biol. Chem. Hoppe-Seyler 371, 589-594.
31. Pepper, D.S. (1992) Some alternative coupling chemistries for affinity chromatography; in Practical Protein Chromatography (Kenney, A. & Fowell, S., eds.) pp. 181-183, The Humana Press, Totowa, New Jersey.
32. Cohen, S.A. & Michaud, D.P. (1993) Synthesis of a fluorescent derivatizing reagent, 6-aminoquinolyl-N-hydroxysuccinimidyl carbamate and its application for the analysis of hydrolysate amino acids via high-performance liquid chromatography. Anal. Biochem. 211, 279-287.