메뉴 건너뛰기




Volumn 35, Issue 3-4, 1999, Pages 349-357

A comparison of biospecific affinity chromatographic methodologies for the purification of NAD+-dependent dehydrogenases: Studies with bovine L- lactate dehydrogenase

Author keywords

Bioaffinity chromatography; Bovine heart L lactate dehydrogenase; Immobilised NAD+ derivatives; Immobilised oxamate; Locking on tactic; Stripping ligand tactic

Indexed keywords

LACTATE DEHYDROGENASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE;

EID: 0033229716     PISSN: 13595113     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0032-9592(99)00078-3     Document Type: Article
Times cited : (5)

References (25)
  • 1
    • 0015334422 scopus 로고
    • General ligands in affinity chromatography: Cofactor-substrate elution of enzymes bound to the immobilised nucleotides adenosine 5′-monophosphate and nicotinamide dinucleotide
    • Mosbach K., Guilford H., Ohlsson R., Scott M. General ligands in affinity chromatography: Cofactor-substrate elution of enzymes bound to the immobilised nucleotides adenosine 5′-monophosphate and nicotinamide dinucleotide. Biochem J. 127:1972;625-631.
    • (1972) Biochem J , vol.127 , pp. 625-631
    • Mosbach, K.1    Guilford, H.2    Ohlsson, R.3    Scott, M.4
  • 2
    • 0015518628 scopus 로고
    • Some applications of insolubilized cofactors to the purification of pyridine nucleotide-dependent dehydrogenases
    • Lowe C.R., Mosbach K., Dean P.D.J. Some applications of insolubilized cofactors to the purification of pyridine nucleotide-dependent dehydrogenases. Biochem Biophys Res Commun. 48:1972;1004-1010.
    • (1972) Biochem Biophys Res Commun , vol.48 , pp. 1004-1010
    • Lowe, C.R.1    Mosbach, K.2    Dean, P.D.J.3
  • 3
    • 0015755909 scopus 로고
    • Affinity chromatography of nicotinamide-adenine dinucleotide-linked dehydrogenases on immobilised derivatives of the dinucleotide
    • Barry S., O'Carra P. Affinity chromatography of nicotinamide-adenine dinucleotide-linked dehydrogenases on immobilised derivatives of the dinucleotide. Biochem J. 135:1973;595-607.
    • (1973) Biochem J , vol.135 , pp. 595-607
    • Barry, S.1    O'Carra, P.2
  • 4
    • 0000747963 scopus 로고
    • Affinity chromatography of lactate dehydrogenase: Model studies demonstrating the potential of the technique in the mechanistic investigation, as well as in the purification, of multisubstrate enzymes
    • O'Carra P., Barry S. Affinity chromatography of lactate dehydrogenase: model studies demonstrating the potential of the technique in the mechanistic investigation, as well as in the purification, of multisubstrate enzymes. FEBS Lett. 21:1972;281-285.
    • (1972) FEBS Lett , vol.21 , pp. 281-285
    • O'Carra, P.1    Barry, S.2
  • 5
    • 0016182225 scopus 로고
    • Lactate dehydrogenase: Specific ligand approach
    • W. Jakoby, Wilchek M. New York: Academic Press
    • O'Carra P., Barry S. Lactate dehydrogenase: specific ligand approach. Jakoby W., Wilchek M. Methods in Enzymology. 34:1974;598-605 Academic Press, New York.
    • (1974) Methods in Enzymology , vol.34 , pp. 598-605
    • O'Carra, P.1    Barry, S.2
  • 6
    • 0031080849 scopus 로고    scopus 로고
    • Both D- and L-specific lactate dehydrogenases co-exist in individual cephalopods
    • Mulcahy P., Cullina A., O'Carra P. Both D- and L-specific lactate dehydrogenases co-exist in individual cephalopods. Comp Biochem Physiol. 116:1997;143-148.
    • (1997) Comp Biochem Physiol , vol.116 , pp. 143-148
    • Mulcahy, P.1    Cullina, A.2    O'Carra, P.3
  • 7
    • 0030955535 scopus 로고    scopus 로고
    • Purification and substrate kinetics of plant lactate dehydrogenase
    • Mulcahy P., O'Carra P. Purification and substrate kinetics of plant lactate dehydrogenase. Phytochemistry. 45:1997;889-896.
    • (1997) Phytochemistry , vol.45 , pp. 889-896
    • Mulcahy, P.1    O'Carra, P.2
  • 8
    • 0025238768 scopus 로고
    • Isozymes of L-lactate dehydrogenase in the squid Loligo vulgaris
    • Mulcahy P., O'Carra P. Isozymes of L-lactate dehydrogenase in the squid Loligo vulgaris. Biochem Soc Trans. 18:1990;270-271.
    • (1990) Biochem Soc Trans , vol.18 , pp. 270-271
    • Mulcahy, P.1    O'Carra, P.2
  • 9
    • 0031077719 scopus 로고    scopus 로고
    • Biospecific affinity purification of octopine dehydrogenase from molluscs
    • Mulcahy P., Griffin T., O'Carra P. Biospecific affinity purification of octopine dehydrogenase from molluscs. Protein Expres Purific. 9:1997;109-114.
    • (1997) Protein Expres Purific , vol.9 , pp. 109-114
    • Mulcahy, P.1    Griffin, T.2    O'Carra, P.3
  • 10
    • 0033082714 scopus 로고    scopus 로고
    • A kinetic locking-on strategy for bioaffinity purification; Further studies with alcohol dehydrogenase
    • O'Flaherty M., McMahon M., Mulcahy P. A kinetic locking-on strategy for bioaffinity purification; further studies with alcohol dehydrogenase. Protein Expres Purific. 15:1999;127-145.
    • (1999) Protein Expres Purific , vol.15 , pp. 127-145
    • O'Flaherty, M.1    McMahon, M.2    Mulcahy, P.3
  • 11
    • 0015713504 scopus 로고
    • A simple general method for the preparation of 6-immobilised analogues of AMP, NAD and of other adenine-containing compounds for affinity chromatography
    • Barry S., O'Carra P. A simple general method for the preparation of 6-immobilised analogues of AMP, NAD and of other adenine-containing compounds for affinity chromatography. FEBS Lett. 37:1973;134-139.
    • (1973) FEBS Lett , vol.37 , pp. 134-139
    • Barry, S.1    O'Carra, P.2
  • 12
    • 0016296445 scopus 로고
    • + and their potential as active coenzymes and affinity adsorbents
    • + and their potential as active coenzymes and affinity adsorbents. Eur J Biochem. 49:1974;511-520.
    • (1974) Eur J Biochem , vol.49 , pp. 511-520
    • Lowe, C.R.1    Mosbach, K.2
  • 14
    • 0016686525 scopus 로고
    • Characteristics of 8-substituted adenine nucleotide derivatives utilised in affinity chromatography
    • Lee C.Y., Kaplan N.O. Characteristics of 8-substituted adenine nucleotide derivatives utilised in affinity chromatography. Arch Biochem Biophys. 168:1975;665-676.
    • (1975) Arch Biochem Biophys , vol.168 , pp. 665-676
    • Lee, C.Y.1    Kaplan, N.O.2
  • 15
    • 0015730613 scopus 로고
    • + analogue, its application in affinity chromatography and as a functioning coenzyme
    • + analogue, its application in affinity chromatography and as a functioning coenzyme. Eur J Biochem. 40:1973;187-193.
    • (1973) Eur J Biochem , vol.40 , pp. 187-193
    • Lindberg, M.1    Larsson, P.O.2    Mosbach, K.3
  • 18
    • 0016220917 scopus 로고
    • + as 'general ligands'
    • W.B. Jakoby, Wilchek M. New York: Academic Press
    • + as 'general ligands'. Jakoby W.B., Wilchek M. Methods in Enzymology. 34:1974;229-242 Academic Press, New York.
    • (1974) Methods in Enzymology , vol.34 , pp. 229-242
    • Mosbach, K.1
  • 19
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of bacteriophage T4. Nature. 227:1970;680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 20
    • 0025773119 scopus 로고
    • The lactate dehydrogenase of the icefish heart: Biochemical adaptations to hypoxia tolerance
    • Feller G., Pauly J.-P., Small A., O'Carra P., Gerday C. The lactate dehydrogenase of the icefish heart: biochemical adaptations to hypoxia tolerance. Biochim Biophys Acta. 1097:1991;343-347.
    • (1991) Biochim Biophys Acta , vol.1097 , pp. 343-347
    • Feller, G.1    Pauly, J.-P.2    Small, A.3    O'Carra, P.4    Gerday, C.5
  • 21
    • 0000469507 scopus 로고
    • Theory and practice of affinity chromatography
    • Epton R. London: Ellis Horwood/Chem Soc
    • O'Carra P. Theory and practice of affinity chromatography. Epton R. Chromatography of Synthetic and Biological Macromolecules. 2:1978;131-158 Ellis Horwood/Chem Soc, London.
    • (1978) Chromatography of Synthetic and Biological Macromolecules , vol.2 , pp. 131-158
    • O'Carra, P.1
  • 23
    • 0033166212 scopus 로고    scopus 로고
    • The kinetic locking-on strategy for bioaffinity purification; further studies with bovine liver glutamate dehydrogenase
    • in press.
    • O'Flaherty M, McMahon M, Forde J, Mulcahy P. The kinetic locking-on strategy for bioaffinity purification; further studies with bovine liver glutamate dehydrogenase. Protein Expres Purific 1999;in press.
    • (1999) Protein Expres Purific
    • O'Flaherty, M.1    McMahon, M.2    Forde, J.3    Mulcahy, P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.