메뉴 건너뛰기




Volumn 19, Issue 6, 2009, Pages 604-609

Potential application of the recombinant Escherichia coli-synthesized heme as a bioavailable iron source

Author keywords

Application; Bioavailability; Iron; Microbial heme

Indexed keywords

ALA SYNTHETASE; DICARBOXYLATE TRANSPORTER; ESCHERICHIA COLI HEME EXTRACT; HEME; IRON; MALATE DEHYDROGENASE (NADP); NATURAL PRODUCT; SYNTHETASE; UNCLASSIFIED DRUG;

EID: 68049101035     PISSN: 10177825     EISSN: 17388872     Source Type: Journal    
DOI: 10.4014/jmb.0810.565     Document Type: Article
Times cited : (16)

References (15)
  • 1
    • 0023653927 scopus 로고
    • Simultaneous determination of hemes a, b, and c from pyridine hemochrome spectra
    • Berry, E. A. and B. L. Trumpower. 1987. Simultaneous determination of hemes a, b, and c from pyridine hemochrome spectra. Anal. Biochem. 161: 1-15.
    • (1987) Anal. Biochem , vol.161 , pp. 1-15
    • Berry, E.A.1    Trumpower, B.L.2
  • 2
    • 0026470429 scopus 로고
    • Contributions of heme and nonheme iron to human nutrition
    • Carpenter, C. E. and A. W. Mahoney. 1992. Contributions of heme and nonheme iron to human nutrition. Crit. Rev. Food Sci. Nutr. 31: 333-367.
    • (1992) Crit. Rev. Food Sci. Nutr , vol.31 , pp. 333-367
    • Carpenter, C.E.1    Mahoney, A.W.2
  • 3
    • 0019739893 scopus 로고
    • Preparation of derivatives of ferrous and ferric hemoglobin
    • Di Iorio, E. E. 1981. Preparation of derivatives of ferrous and ferric hemoglobin. Methods Enzymol. 76: 57-72.
    • (1981) Methods Enzymol , vol.76 , pp. 57-72
    • Di Iorio, E.E.1
  • 4
    • 46449119266 scopus 로고    scopus 로고
    • Expression and purification of intact and functional soybean (Glycine max) seed ferritin complex in Escherichia coli
    • Dong, X., B. Tang, J. Li, Q. Xu, S. Fang, and Z. Hua. 2008. Expression and purification of intact and functional soybean (Glycine max) seed ferritin complex in Escherichia coli. J. Microbiol. Biotechnol. 18: 299-307.
    • (2008) J. Microbiol. Biotechnol , vol.18 , pp. 299-307
    • Dong, X.1    Tang, B.2    Li, J.3    Xu, Q.4    Fang, S.5    Hua, Z.6
  • 5
    • 1642520906 scopus 로고    scopus 로고
    • Bacterial heme biosynthesis and its biotechnological application
    • Frankenberg, N., J. Moser, and D. Jahn. 2003. Bacterial heme biosynthesis and its biotechnological application. Appl. Microbiol. Biotechnol. 63: 115-127.
    • (2003) Appl. Microbiol. Biotechnol , vol.63 , pp. 115-127
    • Frankenberg, N.1    Moser, J.2    Jahn, D.3
  • 6
    • 0030946074 scopus 로고    scopus 로고
    • Purification and characterization of an extracellular heme-binding protein, HasA, involved in heme iron acquisition
    • Izadi, N., Y. Henry, J. Haladjian, M. E. Goldberg, C. Wandersman, M. Delepierre, and A. Lecroisey. 1997. Purification and characterization of an extracellular heme-binding protein, HasA, involved in heme iron acquisition. Biochemistry 36: 7050-7057.
    • (1997) Biochemistry , vol.36 , pp. 7050-7057
    • Izadi, N.1    Henry, Y.2    Haladjian, J.3    Goldberg, M.E.4    Wandersman, C.5    Delepierre, M.6    Lecroisey, A.7
  • 7
    • 36549007021 scopus 로고    scopus 로고
    • The effect of NADP-dependent malic enzyme expression and anaerobic C4 metabolism in Escherichia coli compared with other anaplerotic enzymes
    • Kwon, Y. D., O. H. Kwon, H. S. Lee, and P. Kim. 2007. The effect of NADP-dependent malic enzyme expression and anaerobic C4 metabolism in Escherichia coli compared with other anaplerotic enzymes. J. Appl. Microbiol. 103: 2340-2345.
    • (2007) J. Appl. Microbiol , vol.103 , pp. 2340-2345
    • Kwon, Y.D.1    Kwon, O.H.2    Lee, H.S.3    Kim, P.4
  • 8
    • 33750196846 scopus 로고    scopus 로고
    • Influence of gluconeogenic phosphoenol pyruvate carboxylkinase (PCK) expression on succinic acid fermentation in Escherichia coli under high bicarbonate condition
    • Kwon, Y. D., S. Y. Lee, and P. Kim. 2006. Influence of gluconeogenic phosphoenol pyruvate carboxylkinase (PCK) expression on succinic acid fermentation in Escherichia coli under high bicarbonate condition. J. Microbiol. Biotechnol. 16: 1448-1452.
    • (2006) J. Microbiol. Biotechnol , vol.16 , pp. 1448-1452
    • Kwon, Y.D.1    Lee, S.Y.2    Kim, P.3
  • 9
    • 35348823778 scopus 로고    scopus 로고
    • Cloning and characterization of monofunctional catalase from photosynthetic bacterium Rhodospirillum rubrum S1
    • Lee, D. H., D. C. Oh, Y. S. Oh, J. C. Malinverni, J. J. Kukor, and H. Y. Kahng. 2007. Cloning and characterization of monofunctional catalase from photosynthetic bacterium Rhodospirillum rubrum S1. J. Microbiol. Biotechnol. 17: 1460-1468.
    • (2007) J. Microbiol. Biotechnol , vol.17 , pp. 1460-1468
    • Lee, D.H.1    Oh, D.C.2    Oh, Y.S.3    Malinverni, J.C.4    Kukor, J.J.5    Kahng, H.Y.6
  • 10
    • 0032840418 scopus 로고    scopus 로고
    • The importance of the proportion of heme/nonheme iron in the diet to minimize the interference with calcium, phosphorus, and magnesium metabolism on recovery from nutritional ferropenic anemia
    • Lisbona, F., M. D. Reyes-Andrada, I. Lopez-Aliaga, M. Barrionuevo, M. J. Alferez, and M. S. Campos. 1999. The importance of the proportion of heme/nonheme iron in the diet to minimize the interference with calcium, phosphorus, and magnesium metabolism on recovery from nutritional ferropenic anemia. J. Agric. Food Chem. 47: 2026-2032.
    • (1999) J. Agric. Food Chem , vol.47 , pp. 2026-2032
    • Lisbona, F.1    Reyes-Andrada, M.D.2    Lopez-Aliaga, I.3    Barrionuevo, M.4    Alferez, M.J.5    Campos, M.S.6
  • 11
    • 0027487229 scopus 로고
    • AIN-93 purified diets for laboratory rodents: Final report of the American Institute of Nutrition ad hoc writing committee on the reformulation of the AIN-76A rodent diet
    • Reeves, P. G., F. H. Nielsen, and G. C. Fahey Jr. 1993. AIN-93 purified diets for laboratory rodents: Final report of the American Institute of Nutrition ad hoc writing committee on the reformulation of the AIN-76A rodent diet. J. Nutr. 123: 1939-1951.
    • (1993) J. Nutr , vol.123 , pp. 1939-1951
    • Reeves, P.G.1    Nielsen, F.H.2    Fahey Jr., G.C.3
  • 13
    • 35348834262 scopus 로고    scopus 로고
    • 5-Aminolevulinic acid biosynthesis in Escherichia coli coexpressing NADP-dependent malic enzyme and 5-aminolevulinate synthase
    • Shin, J. A., Y. D. Kwon, O. H. Kwon, H. S. Lee, and P. Kim. 2007. 5-Aminolevulinic acid biosynthesis in Escherichia coli coexpressing NADP-dependent malic enzyme and 5-aminolevulinate synthase. J. Microbiol. Biotechnol. 17: 1579-1584.
    • (2007) J. Microbiol. Biotechnol , vol.17 , pp. 1579-1584
    • Shin, J.A.1    Kwon, Y.D.2    Kwon, O.H.3    Lee, H.S.4    Kim, P.5
  • 14
    • 0014168243 scopus 로고
    • On the orthophenanthroline method of determination of iron in blood serum]. [In Russian.]
    • Volkova, T. N. and N. V. Patrina. 1967. [On the orthophenanthroline method of determination of iron in blood serum]. [In Russian.] Lab. Delo. 2: 97-98.
    • (1967) Lab. Delo , vol.2 , pp. 97-98
    • Volkova, T.N.1    Patrina, N.V.2
  • 15
    • 0025205264 scopus 로고
    • Tetrapyrrole assembly and modification into the ligands of biologically functional cofactors
    • Warren, M. J. and A. I. Scott. 1990. Tetrapyrrole assembly and modification into the ligands of biologically functional cofactors. Trends Biochem. Sci. 15: 486-491.
    • (1990) Trends Biochem. Sci , vol.15 , pp. 486-491
    • Warren, M.J.1    Scott, A.I.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.