Unusual structural characteristics and complete amino acid sequence of a protease inhibitor from Phaseolus acutifolius seeds

Plant Physiology and Biochemistry

Volumn 42, Issue 3, 2004, Pages 209-214

  Campos, Jorge E ^a   Whitaker, John R ^b   Yip, Tai Tung ^c   Hutchens, T William ^c   Blanco Labra, Alejandro ^d  

^a UNIVERSIDAD NACIONAL AUTÓNOMA DE MÉXICO   (Mexico)

^b UNIVERSITY OF CALIFORNIA   (United States)

^c CIPHERGEN BIOSYSTEMS INC   (United States)

^d DEPARTAMENTO DE FÍSICA   (Mexico)

Author keywords

Amino acid sequence; Bowman Birk; High performance liquid chromatography; HPLC; MALDI TOF MS; Matrix assisted laser desorption ionization time of flight mass spectrometry; Metal binding; PAGE; Phaseolus acutifolius; Protease inhibitor; Tepary bean

Indexed keywords

BOWMAN BIRK INHIBITOR; ISOPROTEIN; PROTEINASE INHIBITOR; VEGETABLE PROTEIN;

AMINO ACID SEQUENCE; ARTICLE; BEAN; CHEMISTRY; COMPARATIVE STUDY; ION EXCHANGE CHROMATOGRAPHY; ISOLATION AND PURIFICATION; MOLECULAR GENETICS; PHYLOGENY; PLANT SEED; SEQUENCE HOMOLOGY;

AMINO ACID SEQUENCE; CHROMATOGRAPHY, ION EXCHANGE; MOLECULAR SEQUENCE DATA; PHASEOLUS; PHYLOGENY; PLANT PROTEINS; PROTEASE INHIBITORS; PROTEIN ISOFORMS; SEEDS; SEQUENCE HOMOLOGY, AMINO ACID; TRYPSIN INHIBITOR, BOWMAN-BIRK SOYBEAN;

PHASEOLUS (ANGIOSPERM); PHASEOLUS ACUTIFOLIUS;

EID: 1842587836     PISSN: 09819428     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.plaphy.2003.12.002     Document Type: Article

References (22)

1. Bidlingmeyer B.A., Cohen S.A., Tarvin T.L. Rapid analysis of amino acids using pre-column derivatization. J. Chromat. 336:1984;93-104.
2. Birch N., Southgate B.J., Fellows L.E. Wild and semi-cultivated legumes as potential sources of resistance to bruchid beetles for crop breeder: a study of Vigna/Phaseolus. Wickens G.E., Goodin J.R., Field D.V. Plants of Arid Lands. 1985;303-320 Allen and Unwin, London.
3. Campos J.E., Martinez-Gallardo N., Mendiola-Olaya E., Blanco-Labra A. Purification and partial characterization of a protease inhibitor from Tepary bean (Phaseolus acutifolius) seeds. J. Food Biochem. 21:1997;203-218.
4. Crestfield A.M., Moore S., Stein W.H. Alkylation and identification of the histidine residues at the active site of ribonuclease. J. Biol. Chem. 238:1963;622-627.
5. Gross E., Witkop B. Selective cleavage of the methionyl peptide bonds in ribonuclease with cyanogen bromide. J. Am. Chem. Soc. 83:1961;1510-1511.
6. Hampton B.S., Marshak D.R., Burgees W.H. Structural and functional characterization of full-length heparin-binding growth associated molecule. Mol. Biol. Cell. 3:1992;85-93.
7. Higgins D.G., Sharp P.M. Fast and sensitive multiple alignments on a microcomputer. CABIOS. 5:1989;151-153.
8. Hilder V.A., Gatehouse A.M.R., Sheerman S.E., Baker R.F., Boulter D. A novel mechanism of insect resistance engineered into tobacco. Nature. 330:1987;160-163.
9. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
10. Laskowski M., Kato I. Protein inhibitors of proteases. Annu. Rev. Biochem. 49:1980;593-626.
11. Norioka S., Ikenaka T. Amino acid sequences of trypsin-chymotrypsin inhibitors (A-I, A-II, and B-II) from peanut (Arachis hypogaea): a discussion of the molecular evolution of legume Bowman-Birk type inhibitors. J. Biochem. 94:1983;589-599.
12. Pearson W.R., Lipman D.J. Improved tools for biological sequence comparison. Proc. Natl. Acad. Sci. USA. 85:1988;2444-2448.
13. Ryan C. Protease inhibitors in plants: genes for improving defenses against insects and pathogens. Annu. Rev. Phytopathol. 28:1990;425-449.
14. Saitou N., Nei M. The neighbor-joining method: a new method for reconstructing phylogenetic trees. Mol. Biol. Evol. 4:1987;406-425.
15. Schägger H., Von Jagow G. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for separation of protein in the range of 1 to 100 KDa. Anal. Biochem. 166:1987;368-379.
16. Shade R.E., Pratt R.C., Pomeroy M.A. Development and mortality of the bean weevil, Achanthoscelides obtectus (Coleoptera:Bruchidae), on mature seeds of tepary beans, Phaseolus acutifolius, and common beans Phaseolus vulgaris. Environ. Entomol. 69:1987;1067-1070.
17. Shewry P.R., Lucas J.A. Plant proteins that confer resistance to pest and pathogens. Adv. Bot. Res. 26:1997;135-192.
18. de la Sierra I.L., Quillien L., Flecker P., Gueguen J., Brunie S. Dimeric crystal structure of a Bowman-Birk protease inhibitor from pea seeds. J. Mol. Biol. 285:1999;1195-1207.
19. Suzuki A., Tsunogae Y., Tanaka I., Yamane T., Ashida T., Norioka S., Hara S., Ikenaka T. The structure of a Bowman-Birk type protease inhibitor A-II from peanut (Archis hypogaea) at 3.3 Å resolution. J. Biochem. 101:1987;267-274.
20. Valdes-Rodriguez S., Segura-Nieto M., Chagolla-Lopez A., Vargas-Cortina A., Martinez-Gallardo N., Blanco-Labra A. Purification, characterization, and complete amino acid sequence of a trypsin inhibitor from amaranth (Amaranthus hypocondriacus) seeds. Plant Physiol. 103:1993;1407-1412.
21. Voss R.H., Ermler U., Essen L.O., Wenzl G., Kim Y.M., Flecker P. Crystal structure of the bifunctional soybean Bowman-Birk inhibitor at 0.28-nm resolution. Structural peculiarities in a folded protein conformation. Eur. J. Biochem. 242:1996;122-131.
22. Yip T.T., Van de Water J., Gershwin M.E., Coppel R.L., Hutchens T.W. Cryptic antigenic determinants on the extracellular pyruvate dehydrogenase complex/mimeotope found in primary biliar cirrhosis. A probe by affinity mass spectrometry. J. Biol. Chem. 271:1996;32825-32833.