메뉴 건너뛰기




Volumn 39, Issue 2, 2007, Pages 148-154

Purification and characterization of cytosolic glyceraldehyde-3-phosphate dehydrogenase from the dromedary camel

Author keywords

Camelus dromedarius; Glyceraldehyde 3 phosphate dehydrogenase; Protein purification; Skeletal muscle

Indexed keywords

CAMELUS DROMEDARIUS;

EID: 33846990385     PISSN: 16729145     EISSN: 17457270     Source Type: Journal    
DOI: 10.1111/j.1745-7270.2007.00256.x     Document Type: Article
Times cited : (10)

References (24)
  • 5
    • 0002381906 scopus 로고
    • +-linked glyceraldehyde-3-phosphate dehydrogenase from higher plants
    • Edekmann M, Hallik RB, Chua NH, eds, Amsterdam: Elsevier Biomedical Press
    • +-linked glyceraldehyde-3-phosphate dehydrogenase from higher plants. In: Edekmann M, Hallik RB, Chua NH, eds. Methods in Chloroplast Molecular Biology. Amsterdam: Elsevier Biomedical Press 1982
    • (1982) Methods in Chloroplast Molecular Biology
    • Cerff, R.1
  • 6
    • 0024698882 scopus 로고
    • Cloning and sequence analysis of cDNAs encoding the cytosolic precursors of subunits GapA and GapB of chloroplast glyceraldehyde-3-phosphate dehydrogenase from pea and spinach
    • Brinkman H, Cerff R, Salomon M, Soll J. Cloning and sequence analysis of cDNAs encoding the cytosolic precursors of subunits GapA and GapB of chloroplast glyceraldehyde-3-phosphate dehydrogenase from pea and spinach. Plant Mol Biol 1989, 13: 81-94
    • (1989) Plant Mol Biol , vol.13 , pp. 81-94
    • Brinkman, H.1    Cerff, R.2    Salomon, M.3    Soll, J.4
  • 7
    • 0027729858 scopus 로고
    • ATP-driven transhydrogenation and ionization of water in a reconstituted glyceraldehyde-3-phosphate dehydrogenase (phosphorylating and non-phosphorylating) model system
    • Serrano A, Mateos MI, Losada M. ATP-driven transhydrogenation and ionization of water in a reconstituted glyceraldehyde-3-phosphate dehydrogenase (phosphorylating and non-phosphorylating) model system. Biochem Biophys Res Commun 1993, 197: 1348-1356
    • (1993) Biochem Biophys Res Commun , vol.197 , pp. 1348-1356
    • Serrano, A.1    Mateos, M.I.2    Losada, M.3
  • 8
    • 0002749893 scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase
    • Boyer PD ed, 3rd ed. New York: Academic Press
    • Harris JI, Waters M. Glyceraldehyde-3-phosphate dehydrogenase. In: Boyer PD ed. The Enzymes. 3rd ed. New York: Academic Press 1976
    • (1976) The Enzymes
    • Harris, J.I.1    Waters, M.2
  • 9
    • 0025182490 scopus 로고
    • Extremely thermostable D-glyceraldehyde-3-phosphate dehydrogenase from the eubacterium Thermotoga maritima
    • Wrba A, Schweiger A, Schultes V, Jaenicke R, Zavodsky P. Extremely thermostable D-glyceraldehyde-3-phosphate dehydrogenase from the eubacterium Thermotoga maritima. Biochemistry 1990, 29: 7584-7592
    • (1990) Biochemistry , vol.29 , pp. 7584-7592
    • Wrba, A.1    Schweiger, A.2    Schultes, V.3    Jaenicke, R.4    Zavodsky, P.5
  • 10
    • 0028872557 scopus 로고
    • Characterization of muscle glyceraldehyde-3-phosphate dehydrogenase isoforms from euthermic and induced hibernating Jaculus orientalis
    • Soukri A, Valverde F, Hafid N, Elkebbaj MS, Serrano A. Characterization of muscle glyceraldehyde-3-phosphate dehydrogenase isoforms from euthermic and induced hibernating Jaculus orientalis. Biochim Biophys Acta 1995, 1243: 161-168
    • (1995) Biochim Biophys Acta , vol.1243 , pp. 161-168
    • Soukri, A.1    Valverde, F.2    Hafid, N.3    Elkebbaj, M.S.4    Serrano, A.5
  • 11
    • 0037150030 scopus 로고    scopus 로고
    • +-dependent glyceraldehyde-3-phosphate dehydrogenase in Bacillus cereus
    • +-dependent glyceraldehyde-3-phosphate dehydrogenase in Bacillus cereus. FEMS Microbiol Lett 2002, 211: 29-35
    • (2002) FEMS Microbiol Lett , vol.211 , pp. 29-35
    • Iddar, A.1    Serrano, A.2    Soukri, A.3
  • 12
    • 0031927301 scopus 로고    scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase from Tetrahymena pyriformis: Enzyme purification and characterization of a gap C gene with primitive eukaryotic features
    • Hafid N, Valverde F, Villalobo E, Elkebbaj M, Torres A, Soukri A, Serrano A. Glyceraldehyde-3-phosphate dehydrogenase from Tetrahymena pyriformis: Enzyme purification and characterization of a gap C gene with primitive eukaryotic features. Comp Biochem Physiol B Biochem Mol Biol 1998, B119: 493-503
    • (1998) Comp Biochem Physiol B Biochem Mol Biol , vol.B119 , pp. 493-503
    • Hafid, N.1    Valverde, F.2    Villalobo, E.3    Elkebbaj, M.4    Torres, A.5    Soukri, A.6    Serrano, A.7
  • 13
    • 0000432721 scopus 로고
    • Blue dextran-Sepharose: An affinity column for the dinucleotide fold in proteins
    • Thompson ST, Cass KH, Stellwagen E. Blue dextran-Sepharose: An affinity column for the dinucleotide fold in proteins. Proc Natl Acad Sci USA 1975, 72: 669-672
    • (1975) Proc Natl Acad Sci USA , vol.72 , pp. 669-672
    • Thompson, S.T.1    Cass, K.H.2    Stellwagen, E.3
  • 14
    • 0014310082 scopus 로고
    • Size and charge isomer separation and estimation of molecular weights of proteins by disc gel electrophoresis
    • Hedrick JL, Smith AJ. Size and charge isomer separation and estimation of molecular weights of proteins by disc gel electrophoresis. Arch Biochem Biophys 1968, 162: 155-164
    • (1968) Arch Biochem Biophys , vol.162 , pp. 155-164
    • Hedrick, J.L.1    Smith, A.J.2
  • 15
    • 0036190116 scopus 로고    scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase from the newt Pleurodeles waltl. Protein purification and characterization of a GapC gene
    • Mounaji K, Erraiss NE, Iddar A, Wegnez M, Serrano A, Soukri A. Glyceraldehyde-3-phosphate dehydrogenase from the newt Pleurodeles waltl. Protein purification and characterization of a GapC gene. Comp Biochem Physiol B Biochem Mol Biol 2002, 131: 411-421
    • (2002) Comp Biochem Physiol B Biochem Mol Biol , vol.131 , pp. 411-421
    • Mounaji, K.1    Erraiss, N.E.2    Iddar, A.3    Wegnez, M.4    Serrano, A.5    Soukri, A.6
  • 16
    • 0002219704 scopus 로고
    • The chimeric nature of nuclear genomes and the antiquity of introns as demonstrated by GAPDH gene system
    • Go M, Schimmel P eds, Amsterdam: Elsevier
    • Cerff R. The chimeric nature of nuclear genomes and the antiquity of introns as demonstrated by GAPDH gene system. In: Go M, Schimmel P eds. Tracing Biological Evolution in Protein and Gene Structures. Amsterdam: Elsevier 1995
    • (1995) Tracing Biological Evolution in Protein and Gene Structures
    • Cerff, R.1
  • 17
    • 0030021049 scopus 로고    scopus 로고
    • Evidence for a posttranslational covalent modification of liver glyceraldehyde-3-phosphate dehydrogenase in hibernating jerboa (Jaculus orientalis)
    • Soukri A, Hafid N, Valverde F, Elkebbaj MS, Serrano A. Evidence for a posttranslational covalent modification of liver glyceraldehyde-3-phosphate dehydrogenase in hibernating jerboa (Jaculus orientalis). Biochim Biophys Acta 1996, 1292: 177-187
    • (1996) Biochim Biophys Acta , vol.1292 , pp. 177-187
    • Soukri, A.1    Hafid, N.2    Valverde, F.3    Elkebbaj, M.S.4    Serrano, A.5
  • 18
    • 0020393882 scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase from human tissues
    • Heinz F, Freimuller B. Glyceraldehyde-3-phosphate dehydrogenase from human tissues. Methods Enzymol 1982, 89: 301-305
    • (1982) Methods Enzymol , vol.89 , pp. 301-305
    • Heinz, F.1    Freimuller, B.2
  • 19
    • 0026350705 scopus 로고
    • +-dependent glyceraldehyde-3-phosphate dehydrogenases in Chlorella fusca
    • +-dependent glyceraldehyde-3-phosphate dehydrogenases in Chlorella fusca. Biochem Biophys Res Commun 1991, 181: 1077-1083
    • (1991) Biochem Biophys Res Commun , vol.181 , pp. 1077-1083
    • Serrano, A.1    Mateos, M.I.2    Losada, M.3
  • 20
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM. A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 1976, 72: 248-254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 21
    • 0023473794 scopus 로고
    • Rapid isoelectric focusing in a vertical polyacrylamide minigel system
    • Robertson EF, Dannelly HK, Malloy PJ, Reeves HC. Rapid isoelectric focusing in a vertical polyacrylamide minigel system. Anal Biochem 1987, 167: 290-294
    • (1987) Anal Biochem , vol.167 , pp. 290-294
    • Robertson, E.F.1    Dannelly, H.K.2    Malloy, P.J.3    Reeves, H.C.4
  • 22
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of the head of bacteriophage T4
    • Laemmli UK. Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature 1970, 227: 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 23
    • 0019765424 scopus 로고
    • Production of antisera with small doses of immunogen: Multiple intradermal injections
    • Vaitukaitis JL. Production of antisera with small doses of immunogen: Multiple intradermal injections. Methods Enzymol 1981, 73: 46-52
    • (1981) Methods Enzymol , vol.73 , pp. 46-52
    • Vaitukaitis, J.L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.