Isolation and Characterization of Highly Liganded Protein from Brewer’s Barley Grain

Bioscience, Biotechnology and Biochemistry

Volumn 66, Issue 9, 2002, Pages 1940-1944

  Gorjanović, Stanislava ^a   Cvetković, Ana ^a   Sužnjević, Desanka ^a   Beljanski, Miloš ^a   Vrvić, Miroslav ^b   Hranisavljević, Jovan ^a  

^a Institute of General and Physical Chemistry   (Serbia)

^b UNIVERSITY OF BELGRADE   (Serbia)

Author keywords

Barley grain; Highly liganded proteins; Metal binding proteins; Plant protecting role

Indexed keywords

GLYCOPROTEIN; LIGAND; VEGETABLE PROTEIN;

ARTICLE; BARLEY; CHEMISTRY; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; ISOLATION AND PURIFICATION; MOLECULAR WEIGHT; PLANT SEED; PROTEIN BINDING;

CHROMATOGRAPHY, HIGH PRESSURE LIQUID; GLYCOPROTEINS; HORDEUM; LIGANDS; MOLECULAR WEIGHT; PLANT PROTEINS; PROTEIN BINDING; SEEDS;

HORDEUM; HORDEUM VULGARE; HORDEUM VULGARE SUBSP. VULGARE;

EID: 1842870852     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.66.1940     Document Type: Article

References (18)

1. Chrispeels, M. J., and Raikhel, N. V., Lectins, lectin genes and their role in plant defence. Plant Cell, 3, 1-9 (1991).
2. Pierpoint, W. S., Jackson, P. J., and Evans, R. M., The presence of a thaumatin-like protein, a chitinase, and a glucanase among the pathogenesis-related proteins of potato (Solanum tuberosum). Physiol. Mol. Plant Pathol., 26, 325-338 (1990).
3. Van Loon, L. C., and Van Strien, E. A., The families of pathogenesis-related proteins, their activities, and comparative analysis of PR-1 type proteins. Physiol. Mol. Plant Pathol., 55, 85-97 (1999).
4. Rause, W. E., Structure and function of metal chelators produced by plants: the case for organic acids, amino acids, phytin, and metallothioneins. Cell Biochem. Biophys., 31, 19-48 (1999).
5. Cobbett, C. S., Phytochelatins and their roles in heavy metal detoxification. Plant Physiol., 123, 825-832 (2000).
6. Cvetkovic, A., Gorjanovic, S., Hranisavljevic, J., and Vucelic, D., Isolation and characterization of pathogenesis-related proteins from brewer’s barley grain. J. Serb. Chem. Soc., 62, 51-56 (1997).
7. Cvetkovic, A., Blagojevic, S., and Hranisavljevic, J., Effects of pathogen-related proteins from barley grain on brewers yeast. J. Inst. Brew., 103, 183-186 (1997).
8. Cvetkovic, A., and Hranisavljevic, J., Molecular features in the antifungal activity of thaumatin-like proteins from barley grain. J. Serb. Chem. Soc., 62, 777-786 (1997).
9. Hejgaard, J., Jacobsen, S., and Svendsen, I., Two antifungal thaumatin—like proteins from barley grain. FEBS Lett., 291, 127-131 (1991).
10. Gorjanovic, S., Biologically active glycoproteins from barley grain. M. Sc. thesis, Belgrade University, Faculty of Chemistry, Belgrade (2000).
11. Shewry, P. R., Barley seed proteins. In: “Barley, chemistry and technology”, eds. MacGregor, A. W., and Bhatty, R. S., Am Assoc. Cereal. Chem., St. Paul, MN (1993).
12. Trudel, J., Grenier, J., Potvin, C., and Asselin, A., Several thaumatin-like proteins bind to b-1,3-glucans. Plant Physiol., 118, 1431-1438 (1998).
13. Laemmli, U. K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 277, 680-685 (1970).
14. Weber, M. H., Urinary protein analysis. J. Chro-matogr., 429, 315-344 (1988).
15. Moore, A. T., and Stein, W. H., In “Methods in en-zymology”, eds. Colowick, S. P., and Kaplan, N. O., Academic Press, New York, vol. 6, p. 819 (1963).
16. Dubois, M., Gilles, K. A., Hamilton, J. K., Rebers, P. A., and Smith, F., Colorimetric method for determination of sugars and related substances. Anal. Chem., 28, 350-356 (1956).
17. Mejbaum, W., Estimation of small amounts of pentose especially in derivates of adenylic acid. Hoppe-Seyler’s Z. Physiol. Chem., 258, 117-122 (1939).
18. Suznjevic, D., Erceg, M., and Vucelic, D., Indirect method for quantitative determination of bovine serum albumin and transferin by anodic stripping voltammetry with a rotating glassy carbon electrode. Microchem. J., 69, 59-71 (2001).