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Volumn 63, Issue 5, 1998, Pages 777-781

Purified NADPH-sulfite reductase from Saccharomyces cerevisiae effects on quality of ozonated mackerel surimi

Author keywords

Mackerel surimi; NADPH; Ozonated; Sulfite reductase

Indexed keywords

SACCHAROMYCES CEREVISIAE;

EID: 0031760418     PISSN: 00221147     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1365-2621.1998.tb17898.x     Document Type: Article
Times cited : (11)

References (24)
  • 2
    • 15644373704 scopus 로고
    • The decoloration effect of ozone on swine hemoglobin
    • Taiwan
    • Chang, H.S., Chen C.C., and Chang, H.M. 1995. The decoloration effect of ozone on swine hemoglobin. Food Sci. (Taiwan) 22: 766-775.
    • (1995) Food Sci. , vol.22 , pp. 766-775
    • Chang, H.S.1    Chen, C.C.2    Chang, H.M.3
  • 3
    • 0344394153 scopus 로고    scopus 로고
    • Study on the functional properties of swine hemoglobin decolored with ozone
    • Taiwan
    • Chang, H.S., Chen C.C., and Chang, H.M. 1996. Study on the functional properties of swine hemoglobin decolored with ozone. Food Sci. (Taiwan) 23: 529-537.
    • (1996) Food Sci. , vol.23 , pp. 529-537
    • Chang, H.S.1    Chen, C.C.2    Chang, H.M.3
  • 4
    • 0019860245 scopus 로고
    • Reaction of ozone with sulfhydryls of human erythrocytes
    • Freeman, B.A. and Mudd, J.B. 1981. Reaction of ozone with sulfhydryls of human erythrocytes. Arch. Biochem. Biophy. 208: 212-216.
    • (1981) Arch. Biochem. Biophy. , vol.208 , pp. 212-216
    • Freeman, B.A.1    Mudd, J.B.2
  • 5
    • 0026410002 scopus 로고
    • Structural aspects of metal liganding to functional groups in protein
    • Glusker, J.P. 1991. Structural aspects of metal liganding to functional groups in protein. Adv. Protein Chem. 42:3-66.
    • (1991) Adv. Protein Chem. , vol.42 , pp. 3-66
    • Glusker, J.P.1
  • 6
    • 85008054299 scopus 로고
    • Behavior of the sulfhydryl group of carp actomyosin by heating
    • Itoh, Y., Yoshinaka, Y., and Ikeda, S. 1979. Behavior of the sulfhydryl group of carp actomyosin by heating. Bull. Jap. Soc. Sci. Fish. 45: 1019-1025.
    • (1979) Bull. Jap. Soc. Sci. Fish. , vol.45 , pp. 1019-1025
    • Itoh, Y.1    Yoshinaka, Y.2    Ikeda, S.3
  • 7
    • 85004503526 scopus 로고
    • Formation of polymeric molecules resulting from the intermolecular SS bond formation during gel formation of carp actomyosin by heating
    • Itoh, Y., Yoshinaka, Y., and Ikeda, S. 1980. Formation of polymeric molecules resulting from the intermolecular SS bond formation during gel formation of carp actomyosin by heating. Bull. Jap. Soc. Sci. Fish. 46: 621-624.
    • (1980) Bull. Jap. Soc. Sci. Fish. , vol.46 , pp. 621-624
    • Itoh, Y.1    Yoshinaka, Y.2    Ikeda, S.3
  • 8
    • 50549198780 scopus 로고
    • A micro-Biuret method for estimating proteins
    • Itzhaki, R.F. and Gill, D.M. 1964. A micro-Biuret method for estimating proteins. Anal. Biochem. 9: 401-410.
    • (1964) Anal. Biochem. , vol.9 , pp. 401-410
    • Itzhaki, R.F.1    Gill, D.M.2
  • 10
    • 85010089848 scopus 로고
    • The polymerization of protein through disulfide bonding during the heating of carp myosin
    • Kishi A., S., Itoh, Y., and Obatake, A. 1995. The polymerization of protein through disulfide bonding during the heating of carp myosin. Bull. Jap. Soc. Sci. Fish. 61: 75-80.
    • (1995) Bull. Jap. Soc. Sci. Fish. , vol.61 , pp. 75-80
    • Kishi, A.S.1    Itoh, Y.2    Obatake, A.3
  • 11
    • 0015853344 scopus 로고
    • Maturation of the head of bacteriophage T
    • Laemmli, U. K. and Favre, M. 1973. Maturation of the head of bacteriophage T. J. Med. Biol. 80: 575-579.
    • (1973) J. Med. Biol. , vol.80 , pp. 575-579
    • Laemmli, U.K.1    Favre, M.2
  • 12
    • 15644379012 scopus 로고
    • Effect of ozone treatment on color changes of mackerel (Scomber australasicus) meat
    • Taiwan
    • Lin, K.P. and Chang, H.M. 1994. Effect of ozone treatment on color changes of mackerel (Scomber australasicus) meat. Food Sci. (Taiwan) 21: 312-318.
    • (1994) Food Sci. , vol.21 , pp. 312-318
    • Lin, K.P.1    Chang, H.M.2
  • 13
    • 15644363206 scopus 로고
    • Effect of ozonation on color and functional properties of mackerel (Scomber australasicus) meal
    • Taiwan
    • Lin, K.P. and Chang, H.M. 1995a. Effect of ozonation on color and functional properties of mackerel (Scomber australasicus) meal. Food Sci. (Taiwan) 22: 218-226.
    • (1995) Food Sci. , vol.22 , pp. 218-226
    • Lin, K.P.1    Chang, H.M.2
  • 14
    • 15644364111 scopus 로고
    • Study on the effect of ozonation on color changs mackerel (Scomber australasicus) meat by factorial experimental design
    • Lin, K.P. and Chang, H.M. 1995b. Study on the effect of ozonation on color changs mackerel (Scomber australasicus) meat by factorial experimental design. J. Chinese Agri. Chem. Sci. 32: 262-272.
    • (1995) J. Chinese Agri. Chem. Sci. , vol.32 , pp. 262-272
    • Lin, K.P.1    Chang, H.M.2
  • 16
    • 0023931883 scopus 로고
    • Improved staining of proteins in polyacrylamide gel including isoelectric focusing gels with clear background at nanogram sensitivity using coomassie brilliant blue G-250 and R-250
    • Neuhoff, V., Arold, N., Taube, D., and Ehrhardt, W. 1988. Improved staining of proteins in polyacrylamide gel including isoelectric focusing gels with clear background at nanogram sensitivity using coomassie brilliant blue G-250 and R-250. Electrophoresis 9: 255
    • (1988) Electrophoresis , vol.9 , pp. 255
    • Neuhoff, V.1    Arold, N.2    Taube, D.3    Ehrhardt, W.4
  • 19
    • 0015968302 scopus 로고
    • Reduced nicotinamide adenine dinucleotide phosphate-sulfite reductase of enterobacteria. IV. The Escherichia coli hemoflavoprotein : Subunit structure and dissociation into hemoprotein and flavoprotein components
    • Siegel, L.M. and Davis, P.S. 1974. Reduced nicotinamide adenine dinucleotide phosphate-sulfite reductase of enterobacteria. IV. The Escherichia coli hemoflavoprotein : subunit structure and dissociation into hemoprotein and flavoprotein components. J. Biol. Chem. 249: 1587-1598.
    • (1974) J. Biol. Chem. , vol.249 , pp. 1587-1598
    • Siegel, L.M.1    Davis, P.S.2
  • 20
    • 0015983758 scopus 로고
    • Reduced nicotinamide adenine dinucleotide phosphate-sulfite reductase of enterobacteria. III. The Escherichia coli hemoflavoprotein : Catalytic parameters and the sequence of electron flow
    • Siegel, L.M., Davis, P.S., and Kamin, H. 1974. Reduced nicotinamide adenine dinucleotide phosphate-sulfite reductase of enterobacteria. III. The Escherichia coli hemoflavoprotein : catalytic parameters and the sequence of electron flow. J. Biol. Chem. 249: 1572-1586.
    • (1974) J. Biol. Chem. , vol.249 , pp. 1572-1586
    • Siegel, L.M.1    Davis, P.S.2    Kamin, H.3
  • 21
    • 0015918806 scopus 로고
    • Reduced nicotinamide adenine dinucleotide phosphate-sulfite reductase of enterobacteria. I. The Escherichia coli hemoflavoprotein : Molecular parameters and prosthetic groups
    • Siegel, L.M., Matthew, M.J., and Kamin, H. 1973. Reduced nicotinamide adenine dinucleotide phosphate-sulfite reductase of enterobacteria. I. The Escherichia coli hemoflavoprotein : molecular parameters and prosthetic groups J. Biol. Chem. 248: 251-264.
    • (1973) J. Biol. Chem. , vol.248 , pp. 251-264
    • Siegel, L.M.1    Matthew, M.J.2    Kamin, H.3
  • 22
    • 0000386727 scopus 로고
    • Ferredoxin-sulfite reductase from spinach leaves
    • Tamura, G., Hosoi, T., and Aketagawa, J. 1978. Ferredoxin-sulfite reductase from spinach leaves. Agric. Biol. Chem. 42: 2165-2167.
    • (1978) Agric. Biol. Chem. , vol.42 , pp. 2165-2167
    • Tamura, G.1    Hosoi, T.2    Aketagawa, J.3
  • 23
    • 0014400791 scopus 로고
    • Studies on yeast sulfite reductase I. Purification and characterization
    • Yoshimoto, A. and Sato, R. 1968a. Studies on yeast sulfite reductase I. Purification and characterization. Bioch. Biophy. Acta 153: 555-575.
    • (1968) Bioch. Biophy. Acta , vol.153 , pp. 555-575
    • Yoshimoto, A.1    Sato, R.2
  • 24
    • 0014400792 scopus 로고
    • Studies on yeast sulfite reductase II. Partial purification and properties of genetically incomplete sulfite reductase
    • Yoshimoto, A. and Sato, R. 1968b. Studies on yeast sulfite reductase II. Partial purification and properties of genetically incomplete sulfite reductase. Bioch. Biophy. Acta 153: 576-588.
    • (1968) Bioch. Biophy. Acta , vol.153 , pp. 576-588
    • Yoshimoto, A.1    Sato, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.