Polypeptide Compositions and NH2-terminal Amino Acid Sequences of Proteins in Foxtail and Proso Millets

Bioscience, Biotechnology and Biochemistry

Volumn 63, Issue 11, 1999, Pages 1921-1926

  Kohama, Keiko ^a,b   Nagasawa, Takashi ^a,b   Nishizawa, Naoyuki ^a,b  

^a IWATE INDUSTRIAL RESEARCH INSTITUTE   (Japan)

^b IWATE UNIVERSITY   (Japan)

Author keywords

Homology; Millet; NH2 terminal amino acid sequence; Prolamins

Indexed keywords

PEPTIDE; PEPTIDE FRAGMENT; PROLAMIN PROTEIN, PLANT; VEGETABLE PROTEIN;

AMINO ACID SEQUENCE; ARTICLE; CHEMISTRY; COMPARATIVE STUDY; ISOLATION AND PURIFICATION; MILLET; MOLECULAR GENETICS; MOLECULAR WEIGHT; POLYACRYLAMIDE GEL ELECTROPHORESIS; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY;

AMINO ACID SEQUENCE; ELECTROPHORESIS, POLYACRYLAMIDE GEL; MOLECULAR SEQUENCE DATA; MOLECULAR WEIGHT; PANICUM; PEPTIDE FRAGMENTS; PEPTIDES; PLANT PROTEINS; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID;

EID: 0033217791     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.63.1921     Document Type: Article

References (35)

1. Serna-Saldivar, S. O., McDonough, C. M., and Rooney, L. W., The Millets. In “Handbook of Cereal Science and Technology” (Chapter 6), eds. Lorenz, K. J., and Kulp, K., Marcel Dekker Inc., New York, pp. 271-300 (1991).
2. Dendy, D. A. V., Sorghum and the millets: production and importance. In “Sorghum and Millets Chemistry and Technology” Chapter 2, AACC, St. Paul, pp. 21-26 (1995).
3. Nishizawa, N., Oikawa, M., Nakamura, M., and Hareyama, S., Effect of lysine and threonine supplement on biological value of proso millet protein. Nutr.Rep. Int., 40, 239-245 (1989).
4. Nishizawa, N., Oikawa, M., and Hareyama, S., Effect of dietary protein from proso millet on the plasma cholesterol metabolism in rats. Agric. Biol. Chem., 54, 229-330 (1990).
5. Nishizawa, N., and Fudamoto, Y., The elevation of plasma concentration of high-density lipoprotein cholesterol in mice fed with protein from proso millet. Biosci. Biotechnol. Biochem., 59, 333-335 (1995).
6. Huff, M. W., and Carroll, K. K., Effects of dietary protein on turnover, oxidation and absorption of cholesterol and on steroid excretion in rabbits. J. Lipid. Res., 21, 546-558 (1980).
7. Woodward, C. J. H., and Carrol, K. K., Digestibilities of casein and soya-bean protein in relation to their effects on serum cholesterol in rabbits. Br. J. Nutr., 54, 335-356 (1985).
8. U.S. Department of Agriculture and U.S. Department of Health and Human Services: Nutrition and Your Health: Dietary Guidelines for Americans, 4th ed. (1995).
9. Reichl, D., Extra vascular circulation of lipoproteins: their role in reverse transport of cholesterol. Atherosclerosis, 105, 117-129 (1994).
10. Johnson, W. J., Mahlberg, F. H., Rothblat, G. H., and Philips, M. C., Cholesterol transport between cells and high-density lipoproteins. Biochim. Biophys. Acta, 1085, 273-298 (1991).
11. Pieters, M. N., Schouten, D., and Van Berkel, Th, J. C., In vitro and in vivo evidence for the role of HDL in reverse cholesterol transport. Biochim. Biophys. Acta, 1225, 125-134 (1994).
12. Nagata, Y., Ishiwaki, N., and Sugano, M., Studies on the mechanism of antihypercholesterolemic action of soy protein and soy protein-type amino acid mixture in relation to the casein counterparts in rats. J. Nutr., 12, 1614-1625 (1982).
13. Matsuo, T., and Kimoto, M., The hypocholesterolemic action of the undigested fraction of soybean protein in rats. Atherosclerosis, 72, 115-122 (1988).
14. Taira, H., Studies on amino acid contents in food crops. Eiyo to Shokuryou (in Japanese), 15, 57-61 (1962).
15. Maki, Z., and Tashiro, M., Polypeptide composition of foxtail millet prolamin. Eiyo to Shokuryou (in Japanese), 32, 317-320 (1979).
16. Danno, G., and Natake, M., Isolation of foxtail millet proteins and their subunit structure. Agric. Biol. Chem., 44, 913-918 (1980).
17. Tashiro, M., Chemical and nutritional studies on cereal proteins. Eiyo to Shokuryou (in Japanese), 34, 191-200 (1981).
18. Monterio, P. V., Virpaksha, T. K., and Rao, D. R., Proteins of Italian millet: Amino acid compositions, solubility fractionation and electrophoresis of protein fractions. J. Sci. Food Agric., 33, 1072-1079 (1982).
19. Takumi, K., Udaka, J., Kanoh, M., Koga, T., and Tsuji, H., Polypeptide compositions and antigenic homologies among prolamins from Italian, common and Japanese millet cultivars. J. Sci. Food. Agric., 72, 141-147 (1996).
20. Landry, J., and Moureaux, T., Hetero genetic des glutelins du grain de mais, extraction elective et composition an acids amines des trois fractions isolees. Bull. Soc. Chim. Biol., 52, 1021-1037 (1970).
21. Laemmli, U. K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685 (1970).
22. Moore, S., On the determination of cystine as cysteic acid. J. Biol. Chem., 238, 235-237 (1963).
23. Parameswaran, K. P., and Thayumanavan, B., Homologies between prolamins of different minor millets. Plant Foods for Human Nutrition, 48, 119-126 (1995).
24. Wilson, C. M., Shewry, P. R., and Miflin, B. J., Maize endosperm proteins compared by sodium dodecyl sulfate gel electrophoresis. Cereal Chem., 58, 275-281 (1981).
25. Evans D. J., Schussler, L., and Taylor, J. R. N., Isolation of reduced-soluble protein from sorghum starchy endosperm. J. Cereal Sci., 5, 61-65 (1987).
26. Taylor, J. R. N., Benecke, R. V., and Carlsson, F. H. H., Distribution, purification and N-terminal amino acid sequence of sorghum reduced-soluble protein. J. Cereal Sci., 9, 169-177 (1989).
27. Marks, M. D., and Larkins, B. A., Analysis of sequence microheterogeneity among zein messenger RNAs. J. Biol. Chem., 257, 9976-9983 (1982).
28. Geraghty, D. E., Messing, J., and Rubenstein, I., Sequence analysis and comparison of cDNAs of the zein multigene family. EMBOJ., 1, 1329-1335 (1982).
29. Bietz, J. A., Cereal prolamin evolution and homology related by sequence analysis. Biochemical Genetics., 20, 1039-1053 (1982).
30. Prat, S., Cortadas, J., Puingdomench, P., and Paulau, J., Nucleic acid (cDNA) and amino acid sequences of the maize endosperm protein glutelin-2. Nucl. Acids Res., 13, 1493-1504 (1985).
31. Esen, A., A proposed nomenclature for the alcohol-soluble proteins (zeins) of maize (Zea mays L.). J. Cereal Sci., 5, 117-128 (1987).
32. Paulis, J. W., Disulfide structures of zein proteins from corn endosperm. Cereal Chem., 58, 542-546 (1981).
33. Parameswaran, K. P., and Thayumanavan, B., Isolation and characterization of a 20 kD prolamin from kodo millet (paspa-lum scrobiculatum)(L.): Homology with other millets and cereals. Plant Foods Hum. Nutr., 50, 359-373 (1997).
34. Wang, J. Y., Fujimoto, K., Miyazawa, T., and Endo, Y., An-tioxidative mechanism of maize zein in powder model systems against methyl linoleate: Effect of water activity and coexistence of antioxidants. J. Agric. Food Chem., 39, 351-355 (1991).
35. Matsumura, Y., Andonova, P. P., Hayashi, Y., Murakami, H., and Mori, T., Antioxidant activities of zeins from different maize varieties against docosahexanoic acid ethyl ester. Cereal Chem., 71, 428-433 (1994).