Warianty tytułu
Języki publikacji
Abstrakty
Two serine proteinase inhibitors (ELTII and ELT1II) have been isolated from mature seeds of Echinocystis lobata by ammonium sulfate fractionation, methanol precipitation, ion exchange chromatography, affinity chromatography on immobilized anhydrotrypsin and HPLC. ELTI I and ELTI II consist of 33 and 29 amino-acid residues, respectively. The primary structures of these inhibitors are as follows: ELTI I KEEQRVCPRILMRCKRDSDCLAQCTCQQSGFCG ELTI II RVCPRILMRCKRDSDCLAQCTCQQSGFCG The inhibitors show sequence similarity with the squash inhibitor family. ELTI I differs from ELTI II only by the presence of the NH2-terminal tetrapeptide Lys- -Glu-Glu-Gln. The association constants (Ka) of F.LTI I and ELTI II with bovine-trypsin were determined to be 6.6 x 1010 M -1 and 3.1 x 1011 M -1, whereas the association constants of these inhibitors with cathepsin G were 1.2 x 107 M -1 and 1.1 x 107 M -1, respectively.
Wydawca
Czasopismo
Rocznik
Tom
Numer
Opis fizyczny
p.507-513,fig.
Twórcy
autor
- University of Wroclaw, Tamka 2, 50-137 Wroclaw, Poland
autor
autor
autor
Bibliografia
- 1. Polanowski, A., Wilusz, T., Nienartowicz, B., Cie^Iar, E., Slomiriska, 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. lioppe-Seyler 368,1505-1507.
- 4. Joubert, F.J. (1984) Trypsin isoinhibitors from Momordica repens seeds. Phytochemistry 23, 1401-1406.
- 5. Heitz, A., Chiche, L., Le-Nguyen, D. & Castro, B. (1989) 'h 2D NMK 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. Common Makino) seeds. Biosci. Biotech. Biochem. 56, 1241-1246.
- 7. I.ee, Ch.-F. & Lin, J.-Y. (1995) Amino acid sequences of trypsin inhibitors from the melon Cucumis melo. /. 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 DN A 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. 1 lama to, 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 A resolution crystal structure of the complex formed between porcine (J-trypsin and CMTI-A, a trypsin inhibitor of the squash family. Detailed comparison with bovine P-trypsin and its complex. /. Mol. Biol. 229,1022-1036.
- 15. Bode, W., Greyling, H.J., Huber, R.,Otlewski, J. & Wilusz, T. (1989) The refined 2.0 A X-ray crystal structure of the complex formed between bovine ^-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. Likos, J.J. (1989) 'H-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. /. Mol. Biol. 210,635-648.
- 18. Krishnamoorthi, R. & Sun Lin Ch.-L. (1992) Structural consequences of the natural substitution, K9K, 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 7ft- chosanthes trypsin inhibitor — a squash family inhibitor. J. Biochem. (Tokyo) 112,45-51.
- 20. Rolka, K., Kuprys2ewski, G., Ragnarsson, U., Otlewski, J., Krokoszynska, I. & Wilusz, T. (1991) Chemical synthesis of new trypsin, chymo- trypsin and elastase inhibitors by amino-acid substitution in a trypsin inhibitor from squash seeds (CMTI III) Biol. Chem. Hoppe-Scyler 372, 63-68.
- 21. Bolewska, K., Krowarsch, D., Otlewski, J., Jaro- szewski, L. & Bierzynski, A. (1995) Synthesis, cloning and expression in Escherichia coli of a gene coding for the Met8^Leu CMTI I — a representative of the squash inhibitors of serine proteinases. FEBS Lett. 377,172-174.
- 22. Rempola, 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-Katzenellen- bogen, W. (1978) A simple method for isolating trypsin from trichloroacetic acid extracts of bovine pancreas. Anal. Biochem. 90,816-820.
- 24. Iiepniecks, J.J. & Light, A. (1974) Preparation of p-trypsin by affinity chromatography of entero- kinase-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 HC1. 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. Bio- chetn. Biophys. 95,271-278.
- 28. Wtorek, W., Polanowski, A. & Wilusz, T. (1996) Tne use of sequencial affinity chromatography for separation of human neutrophil elastase, cathepsinG 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., Krokoszyriska, 1. & 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. & Howell, $., eds.) pp. 181-183, The I Iumana Press, Totowa, New Jersey.
- 32. Cohen, S.A. & Michaud, D.P. (1993) Synthesis of a fluorescent derivatizing reagent, 6-amino- quinolyl-N-hydroxysuccinimidyl carbamate and its application for the analysis of hydro- lysate amino acids via high-performance liquid chromatography. Anal. Biochem. 211,279-287.
Typ dokumentu
Bibliografia
Identyfikatory
Identyfikator YADDA
bwmeta1.element.agro-article-3e5c4b8a-cd83-4e3e-abdb-6f190c762e3a