메뉴 건너뛰기




Volumn 107, Issue , 2015, Pages 50-55

Myoglobin extraction from mammalian skeletal muscle and oxygen affinity determination under physiological conditions

Author keywords

Anion exchange chromatography; Myoglobin; Oxygen affinity; Oxygen dissociation

Indexed keywords

AVES; BOS TAURUS; BOVINAE; EQUIDAE; MAMMALIA; VERTEBRATA;

EID: 84917706051     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2014.11.004     Document Type: Article
Times cited : (16)

References (45)
  • 2
    • 6344277177 scopus 로고    scopus 로고
    • Myoglobin: An essential hemoprotein in striated muscle
    • G.A. Ordway, and D.J. Garry Myoglobin: an essential hemoprotein in striated muscle J. Exp. Biol. 207 2004 3441 3446
    • (2004) J. Exp. Biol. , vol.207 , pp. 3441-3446
    • Ordway, G.A.1    Garry, D.J.2
  • 3
    • 77955650019 scopus 로고    scopus 로고
    • Myoglobin's old and new clothes: From molecular structure to function in living cells
    • G. Gros, B.A. Wittenberg, and T. Jue Myoglobin's old and new clothes: from molecular structure to function in living cells J. Exp. Biol. 213 2010 2713 2725
    • (2010) J. Exp. Biol. , vol.213 , pp. 2713-2725
    • Gros, G.1    Wittenberg, B.A.2    Jue, T.3
  • 4
    • 84891892356 scopus 로고    scopus 로고
    • A review of the multi-level adaptations for maximizing aerobic dive duration in marine mammals: From biochemistry to behavior
    • R.W. Davis A review of the multi-level adaptations for maximizing aerobic dive duration in marine mammals: from biochemistry to behavior J. Comp. Physiol. B. 184 2014 23 53
    • (2014) J. Comp. Physiol. B. , vol.184 , pp. 23-53
    • Davis, R.W.1
  • 7
    • 0041806720 scopus 로고    scopus 로고
    • Myoglobin: The hydrogen atom of biology and a paradigm of complexity
    • H. Frauenfelder, B.H. McMahon, and P.W. Fenimore Myoglobin: The hydrogen atom of biology and a paradigm of complexity Proc. Natl. Acad. Sci. 100 2003 8615 8617
    • (2003) Proc. Natl. Acad. Sci. , vol.100 , pp. 8615-8617
    • Frauenfelder, H.1    McMahon, B.H.2    Fenimore, P.W.3
  • 8
    • 76749086030 scopus 로고    scopus 로고
    • Myoglobin strikes back
    • M. Brunori Myoglobin strikes back Prot. Sci. 19 2010 195 201
    • (2010) Prot. Sci. , vol.19 , pp. 195-201
    • Brunori, M.1
  • 9
    • 79958043184 scopus 로고    scopus 로고
    • Phylogenetic diversification of the globin gene superfamily in chordates
    • J.F. Storz, J.C. Opazo, and F.G. Hoffmann Phylogenetic diversification of the globin gene superfamily in chordates IUBMB Life 63 2011 313 322
    • (2011) IUBMB Life , vol.63 , pp. 313-322
    • Storz, J.F.1    Opazo, J.C.2    Hoffmann, F.G.3
  • 10
    • 84873096226 scopus 로고    scopus 로고
    • Gene duplication, genome duplication, and the functional diversification of vertebrate globins
    • J.F. Storz, J.C. Opazo, and F.G. Hoffmann Gene duplication, genome duplication, and the functional diversification of vertebrate globins Mol. Phylogenet. Evol. 66 2013 469 478
    • (2013) Mol. Phylogenet. Evol. , vol.66 , pp. 469-478
    • Storz, J.F.1    Opazo, J.C.2    Hoffmann, F.G.3
  • 11
    • 0021876589 scopus 로고
    • Rapid separation and identification of myoglobin and hemoglobin in urine by centrifugation through a microconcentrator membrane
    • M.J. Kelner, and N.M. Alexander Rapid separation and identification of myoglobin and hemoglobin in urine by centrifugation through a microconcentrator membrane Clin. Chem. 31 1985 112 114
    • (1985) Clin. Chem. , vol.31 , pp. 112-114
    • Kelner, M.J.1    Alexander, N.M.2
  • 13
    • 84958111940 scopus 로고
    • The absorption spectra and extinction coefficients of myoglobin
    • W.J. Bowen The absorption spectra and extinction coefficients of myoglobin J. Biol. Chem. 179 1949 235 245
    • (1949) J. Biol. Chem. , vol.179 , pp. 235-245
    • Bowen, W.J.1
  • 14
    • 0015185336 scopus 로고
    • The detection of myoglobin in urine and its distinction from normal and variant haemoglobins
    • F.E. Boulton, and R.G. Huntsman The detection of myoglobin in urine and its distinction from normal and variant haemoglobins J. Clin. Pathol. 24 1971 816 821
    • (1971) J. Clin. Pathol. , vol.24 , pp. 816-821
    • Boulton, F.E.1    Huntsman, R.G.2
  • 15
    • 0030306558 scopus 로고    scopus 로고
    • Some observations on the absorption spectra of various myoglobin derivatives found in meat
    • S.J. Millar, B.W. Moss, and M.H. Stevenson Some observations on the absorption spectra of various myoglobin derivatives found in meat Meat Sci. 42 1996 277 288
    • (1996) Meat Sci. , vol.42 , pp. 277-288
    • Millar, S.J.1    Moss, B.W.2    Stevenson, M.H.3
  • 16
    • 0000754869 scopus 로고
    • The absorption spectra of hemoglobin and its derivatives in the visible and near infra-red regions
    • B.L. Horecker The absorption spectra of hemoglobin and its derivatives in the visible and near infra-red regions J. Biol. Chem. 148 1943 173 183
    • (1943) J. Biol. Chem. , vol.148 , pp. 173-183
    • Horecker, B.L.1
  • 17
    • 0026005327 scopus 로고
    • Absorption spectra of human fetal and adult oxyhemoglobin, de-oxyhemoglobin, carboxyhemoglobin, and methemoglobin
    • W.G. Zijlstra, A. Buursma, and W.P. Meeuwsen-Van der Roest Absorption spectra of human fetal and adult oxyhemoglobin, de-oxyhemoglobin, carboxyhemoglobin, and methemoglobin Clin. Chem. 37 1991 1633 1638
    • (1991) Clin. Chem. , vol.37 , pp. 1633-1638
    • Zijlstra, W.G.1    Buursma, A.2    Meeuwsen-Van Der Roest, W.P.3
  • 18
    • 0031425663 scopus 로고    scopus 로고
    • Spectrophotometry of hemoglobin: Absorption spectra of bovine oxyhemoglobin, deoxyhemoglobin, carboxyhemoglobin, and methemoglobin
    • W.G. Zijlstra, and A. Buursma Spectrophotometry of hemoglobin: absorption spectra of bovine oxyhemoglobin, deoxyhemoglobin, carboxyhemoglobin, and methemoglobin Comp. Biochem. Physiol. B 118 1997 743 749
    • (1997) Comp. Biochem. Physiol. B , vol.118 , pp. 743-749
    • Zijlstra, W.G.1    Buursma, A.2
  • 20
    • 80052659359 scopus 로고    scopus 로고
    • Bridging the gap between chemistry, physiology, and evolution: Quantifying the functionality of sperm whale myoglobin mutants
    • P. Dasmeh, and K.P. Kepp Bridging the gap between chemistry, physiology, and evolution: quantifying the functionality of sperm whale myoglobin mutants Comp. Biochem. Physiol. A 161 2012 9 17
    • (2012) Comp. Biochem. Physiol. A , vol.161 , pp. 9-17
    • Dasmeh, P.1    Kepp, K.P.2
  • 21
    • 84870168733 scopus 로고    scopus 로고
    • Aerobic dive limits of seals with mutant myoglobin using combined thermochemical and physiological data
    • P. Dasmeh, R.W. Davis, and K.P. Kepp Aerobic dive limits of seals with mutant myoglobin using combined thermochemical and physiological data Comp. Biochem. Physiol. 164A 2012 119 128
    • (2012) Comp. Biochem. Physiol. , vol.164 A , pp. 119-128
    • Dasmeh, P.1    Davis, R.W.2    Kepp, K.P.3
  • 23
    • 34547953953 scopus 로고    scopus 로고
    • Ligand pathways in myoglobin: A review of Trp cavity mutations
    • J.S. Olson, J. Soman, and G.N. Phillips Ligand pathways in myoglobin: a review of Trp cavity mutations IUBMB Life 59 2008 552 562
    • (2008) IUBMB Life , vol.59 , pp. 552-562
    • Olson, J.S.1    Soman, J.2    Phillips, G.N.3
  • 24
    • 0024350819 scopus 로고
    • Comparative oxygen affinity of fish and mammalian myoglobins
    • J.W. Nichols, and L.J. Weber Comparative oxygen affinity of fish and mammalian myoglobins J. Comp. Physiol. B. 159 1989 205 209
    • (1989) J. Comp. Physiol. B. , vol.159 , pp. 205-209
    • Nichols, J.W.1    Weber, L.J.2
  • 26
    • 84866241609 scopus 로고    scopus 로고
    • Functional properties of myoglobins from five whale species with different diving capacities
    • S. Helbo, and A. Fago Functional properties of myoglobins from five whale species with different diving capacities J. Exp. Biol. 215 2012 3403 3410
    • (2012) J. Exp. Biol. , vol.215 , pp. 3403-3410
    • Helbo, S.1    Fago, A.2
  • 28
    • 0001784483 scopus 로고
    • Total pigments and myoglobin concentration in four bovine muscles
    • D.A. Rickansrud, and R.L. Henrickson Total pigments and myoglobin concentration in four bovine muscles J. Food Sci. 32 1967 57 61
    • (1967) J. Food Sci. , vol.32 , pp. 57-61
    • Rickansrud, D.A.1    Henrickson, R.L.2
  • 29
    • 84986512480 scopus 로고
    • Hemoglobin, myoglobin, and total pigments in beef and chicken muscles: Chromatographic determination
    • D. Han, K.W. McMillin, and J.S. Godber Hemoglobin, myoglobin, and total pigments in beef and chicken muscles: chromatographic determination J. Food Sci. 59 1994 1279 1282
    • (1994) J. Food Sci. , vol.59 , pp. 1279-1282
    • Han, D.1    McMillin, K.W.2    Godber, J.S.3
  • 30
    • 0019395833 scopus 로고
    • Kinetic analysis of myoglobin autoxidation by isoelectric-focusing electrophoresis
    • A. Tomoda, T. Takizawa, A. Tsuji, and Y. Yoneyama Kinetic analysis of myoglobin autoxidation by isoelectric-focusing electrophoresis Biochem. J. 193 1981 181 185
    • (1981) Biochem. J. , vol.193 , pp. 181-185
    • Tomoda, A.1    Takizawa, T.2    Tsuji, A.3    Yoneyama, Y.4
  • 31
    • 0000780698 scopus 로고
    • Influence of temperature, pH, and phospholipid composition upon the stability of myoglobin and phospholipid: A liposome model
    • M.C. Yin, and C. Faustman Influence of temperature, pH, and phospholipid composition upon the stability of myoglobin and phospholipid: a liposome model J. Agric. Food Chem. 41 1993 853 857
    • (1993) J. Agric. Food Chem. , vol.41 , pp. 853-857
    • Yin, M.C.1    Faustman, C.2
  • 32
    • 0037165564 scopus 로고    scopus 로고
    • Temperature and pH dependence of the autoxidation rate of bovine, ovine, porcine, and cervine oxymyoglobin isolated from three different muscles - Longissimus dorsi, Bluteus medius, and Biceps femoris
    • D. Gutzke, and G.R. Trout Temperature and pH dependence of the autoxidation rate of bovine, ovine, porcine, and cervine oxymyoglobin isolated from three different muscles - Longissimus dorsi, Bluteus medius, and Biceps femoris J. Agric. Food Chem. 50 2002 2673 2678
    • (2002) J. Agric. Food Chem. , vol.50 , pp. 2673-2678
    • Gutzke, D.1    Trout, G.R.2
  • 33
    • 0030819158 scopus 로고    scopus 로고
    • Kinetic characterization of myoglobins from vertebrates with vastly different body temperatures
    • R.E. Cashon, M.E. Vayda, and B.D. Sidell Kinetic characterization of myoglobins from vertebrates with vastly different body temperatures Comp. Biochem. Physiol. 117B 1997 613 620
    • (1997) Comp. Biochem. Physiol. , vol.117 B , pp. 613-620
    • Cashon, R.E.1    Vayda, M.E.2    Sidell, B.D.3
  • 34
    • 0018290896 scopus 로고
    • Metmyoglobin reductase. Identification and purification of a reduced nicotinamide adenine dinucleotide-dependent enzyme from bovine heart which reduces metmyoglobin
    • L. Hagler, R.I. Coppes Jr, and R.H. Herman Metmyoglobin reductase. Identification and purification of a reduced nicotinamide adenine dinucleotide-dependent enzyme from bovine heart which reduces metmyoglobin J. Biol. Chem. 254 1979 6505 6514
    • (1979) J. Biol. Chem. , vol.254 , pp. 6505-6514
    • Hagler, L.1    Coppes, R.I.2    Herman, R.H.3
  • 35
    • 0001339975 scopus 로고
    • Chromatography of myoglobin on diethylaminoethyl cellulose columns
    • W.D. Brown Chromatography of myoglobin on diethylaminoethyl cellulose columns J. Biol. Chem. 236 1961 2238 2240
    • (1961) J. Biol. Chem. , vol.236 , pp. 2238-2240
    • Brown, W.D.1
  • 36
    • 0000456481 scopus 로고
    • Preparation of crystalline oxymyoglobin from horse heart
    • I. Yamazaki, K. Yokota, and K. Shikama Preparation of crystalline oxymyoglobin from horse heart J. Biol. Chem. 239 1964 4151 4153
    • (1964) J. Biol. Chem. , vol.239 , pp. 4151-4153
    • Yamazaki, I.1    Yokota, K.2    Shikama, K.3
  • 40
    • 0028817948 scopus 로고
    • Performance characteristics of Hemox-analyzer for assessment of the hemoglobina dissociation curve
    • R. Guarnone, E. Centenara, and G. Barosi Performance characteristics of Hemox-analyzer for assessment of the hemoglobina dissociation curve Haematologica 80 1995 426 430
    • (1995) Haematologica , vol.80 , pp. 426-430
    • Guarnone, R.1    Centenara, E.2    Barosi, G.3
  • 41
    • 84874724662 scopus 로고    scopus 로고
    • Update on activities at the Universal Protein Resource (UniProt) in 2013
    • UniProt Consortium Update on activities at the Universal Protein Resource (UniProt) in 2013 Nucleic Acids Res. 41 2013 D43 D47
    • (2013) Nucleic Acids Res. , vol.41 , pp. 43-D47
    • Consortium, U.1
  • 42
    • 65449188232 scopus 로고    scopus 로고
    • Jalview Version 2-A multiple sequence alignment editor and analysis workbench
    • A.M. Waterhouse, J.B. Procter, D.M. Martin, M. Clamp, and G.J. Barton Jalview Version 2-a multiple sequence alignment editor and analysis workbench Bioinformatics 25 2009 1189 1191
    • (2009) Bioinformatics , vol.25 , pp. 1189-1191
    • Waterhouse, A.M.1    Procter, J.B.2    Martin, D.M.3    Clamp, M.4    Barton, G.J.5
  • 45
    • 84887617938 scopus 로고    scopus 로고
    • Molecular cloning, characterization and expression of myoglobin in Tibetan antelope (Pantholops hodgsonii), a species with hypoxic tolerance
    • L. Ma, X. Shao, Y. Wang, Y. Yang, Z. Bai, Y. Zhao, G. Jin, Q. Ga, Q. Yang, and R. Gi Molecular cloning, characterization and expression of myoglobin in Tibetan antelope (Pantholops hodgsonii), a species with hypoxic tolerance Gene 533 2013 532 537
    • (2013) Gene , vol.533 , pp. 532-537
    • Ma, L.1    Shao, X.2    Wang, Y.3    Yang, Y.4    Bai, Z.5    Zhao, Y.6    Jin, G.7    Ga, Q.8    Yang, Q.9    Gi, R.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.