메뉴 건너뛰기




Volumn 414, Issue , 1997, Pages 19-27

Human corneal and lens aldehyde dehydrogenases: Purification and properties of human lens ALDH1 and differential expression as major soluble proteins in human lens (ALDH1) and cornea (ALDH3)

Author keywords

[No Author keywords available]

Indexed keywords

ALDEHYDE DEHYDROGENASE; ISOENZYME;

EID: 0030907192     PISSN: 00652598     EISSN: None     Source Type: Book Series    
DOI: None     Document Type: Conference Paper
Times cited : (35)

References (38)
  • 1
    • 0025039523 scopus 로고
    • Bovine corneal aldehyde dehydrogenase: The major soluble corneal protein with a possible dual protective role for the eye
    • Abedinia, M., Pain, T., Algar, E.M. and Holmes, R.S.: Bovine corneal aldehyde dehydrogenase: the major soluble corneal protein with a possible dual protective role for the eye. Exp. Eye Res. 51 (1990) 419-426.
    • (1990) Exp. Eye Res. , vol.51 , pp. 419-426
    • Abedinia, M.1    Pain, T.2    Algar, E.M.3    Holmes, R.S.4
  • 2
    • 0019464436 scopus 로고
    • Isolation and characterization of BCP54 the major soluble protein of bovine cornea
    • Alexander, R.J., Silverman, B. and Henley, W.L.: Isolation and characterization of BCP54 the major soluble protein of bovine cornea. Exp. Eye Res. 32 (1981) 205-216.
    • (1981) Exp. Eye Res. , vol.32 , pp. 205-216
    • Alexander, R.J.1    Silverman, B.2    Henley, W.L.3
  • 3
    • 0024585490 scopus 로고
    • Kinetic properties of murine liver aldehyde dehydrogenases
    • Weiner, H. and Flynn, T.G. (Eds.), Alan R. Liss, N.Y.
    • Algar, E.M. and Holmes, R.S.: Kinetic properties of murine liver aldehyde dehydrogenases. In Weiner, H. and Flynn, T.G. (Eds.), Enzymology and Molecular Biology of Carbonyl Metabolism 2. Alan R. Liss, N.Y., 1989 pp >93-103.
    • (1989) Enzymology and Molecular Biology of Carbonyl Metabolism , vol.2 , pp. 93-103
    • Algar, E.M.1    Holmes, R.S.2
  • 4
    • 0025785329 scopus 로고
    • Human aldehyde dehydrogenase activity with aldehyde metabolites of monoamine, diamines and polyamines
    • Ambroziak, W. and Pietruszko, R.: Human aldehyde dehydrogenase activity with aldehyde metabolites of monoamine, diamines and polyamines. J. Biol. Chem. 266 (1991) 13011-13018.
    • (1991) J. Biol. Chem. , vol.266 , pp. 13011-13018
    • Ambroziak, W.1    Pietruszko, R.2
  • 5
    • 0015986813 scopus 로고
    • Resolution of bacterial proteins by polyacrylamide gel electrophoresis on slabs
    • Ames, G.F.-I.: Resolution of bacterial proteins by polyacrylamide gel electrophoresis on slabs. J. Biol. Chem. 249 (1974) 634-644.
    • (1974) J. Biol. Chem. , vol.249 , pp. 634-644
    • Ames, G.F.-I.1
  • 6
    • 0029868332 scopus 로고    scopus 로고
    • Constitutive expression of class 3 aldehyde dehydrogenase in cultured rat epithelium
    • Boesch, J.S., Lee, C. and Lindahl, R.G.: Constitutive expression of class 3 aldehyde dehydrogenase in cultured rat epithelium. J. Biol. Chem.271 (1996) 5150-5157.
    • (1996) J. Biol. Chem. , vol.271 , pp. 5150-5157
    • Boesch, J.S.1    Lee, C.2    Lindahl, R.G.3
  • 8
    • 0026063533 scopus 로고
    • Bovine corneal protein 54K (BCP54) is a homologue of the tumour-associated (Class 3) rat aldehyde dehydrogenase (RATALD)
    • Cooper, D.L., Bapist, E.W., Enghild, J., Lee, H., Isola, N. and Klintworth, G. K.: Bovine corneal protein 54K (BCP54) is a homologue of the tumour-associated (Class 3) rat aldehyde dehydrogenase (RATALD). Gene 98 (1991) 201-207.
    • (1991) Gene , vol.98 , pp. 201-207
    • Cooper, D.L.1    Bapist, E.W.2    Enghild, J.3    Lee, H.4    Isola, N.5    Klintworth, G.K.6
  • 9
    • 0027503116 scopus 로고
    • Members of the ALDH gene family are lens and corneal crystallins
    • Weiner, H., Crabb, D.W., and Flynn, G.F. (Eds.), Plenum Press, New York
    • Cooper D.L., Isola N.R., Stevenson K. and Baptist E.W.: Members of the ALDH gene family are lens and corneal crystallins. In Weiner, H., Crabb, D.W., and Flynn, G.F. (Eds.), Enzymology and Molecular Biology of Carbonyl Metabolism 4. Plenum Press, New York, 1993, pp 169-179.
    • (1993) Enzymology and Molecular Biology of Carbonyl Metabolism , vol.4 , pp. 169-179
    • Cooper, D.L.1    Isola, N.R.2    Stevenson, K.3    Baptist, E.W.4
  • 10
    • 0026390277 scopus 로고
    • Aldehdye dehydrogenase, aldose reductase and free radical scavengers in cataract
    • Crabbe, M.J.C. and Hoe, S.T.: Aldehdye dehydrogenase, aldose reductase and free radical scavengers in cataract. Enzyme 45 (1991)188-193
    • (1991) Enzyme , vol.45 , pp. 188-193
    • Crabbe, M.J.C.1    Hoe, S.T.2
  • 11
    • 0026667068 scopus 로고
    • Identification of human liver aldehyde dehydrogenases that catalyse the oxidation of aldophosphamide and retinaldehyde
    • Dockham, P.A., Lee, M.-O. and Sladek, N.E.: Identification of human liver aldehyde dehydrogenases that catalyse the oxidation of aldophosphamide and retinaldehyde. Biochem. Pharmacol. 43 (1992) 2453-2469.
    • (1992) Biochem. Pharmacol. , vol.43 , pp. 2453-2469
    • Dockham, P.A.1    Lee, M.-O.2    Sladek, N.E.3
  • 12
    • 0024464690 scopus 로고
    • Characterisation of rat cornea aldehyde dehydrogenase
    • Evces, S. and Lindahl, R.: Characterisation of rat cornea aldehyde dehydrogenase. Arch. Biochem. Biophys. 274 (1989) 518-529.
    • (1989) Arch. Biochem. Biophys. , vol.274 , pp. 518-529
    • Evces, S.1    Lindahl, R.2
  • 13
    • 0015499904 scopus 로고
    • Horse liver aldehyde dehydrogenase 1. Purification and characterization
    • Feldman, R.I. and Weiner, H.: Horse liver aldehyde dehydrogenase 1. Purification and characterization. J. Biol. Chem. 247 (1972) 260-266.
    • (1972) J. Biol. Chem. , vol.247 , pp. 260-266
    • Feldman, R.I.1    Weiner, H.2
  • 15
    • 0017406798 scopus 로고
    • Two aldehyde dehydrogenases from human liver isolation via affinity chromatography and characterization of the isozymes
    • Greenfield, N.J. and Pietruszko, R.: Two aldehyde dehydrogenases from human liver isolation via affinity chromatography and characterization of the isozymes. Biochim. Biophys. Acta 483 (1977) 35-45.
    • (1977) Biochim. Biophys. Acta , vol.483 , pp. 35-45
    • Greenfield, N.J.1    Pietruszko, R.2
  • 16
    • 0019945001 scopus 로고
    • Human aldehyde dehydrogenase: Improved purification procedure and comparison of homogeneous isoenzymes E1 and E2
    • Hempel J.D., Reed, D.N. and Pietruszko, R.: Human aldehyde dehydrogenase: improved purification procedure and comparison of homogeneous isoenzymes E1 and E2. Alcoholism: Clinical and Experimental Research 6 (1982) 417-425.
    • (1982) Alcoholism: Clinical and Experimental Research , vol.6 , pp. 417-425
    • Hempel, J.D.1    Reed, D.N.2    Pietruszko, R.3
  • 17
    • 0022443289 scopus 로고
    • Ocular NAD-dependent alcohol dehydrogenase and aldehyde dehydrogenase in the baboon
    • Holmes, R.S. and VandeBerg, J.L.: Ocular NAD-dependent alcohol dehydrogenase and aldehyde dehydrogenase in the baboon. Exp. Eye Res. 43 (1986) 383-396.
    • (1986) Exp. Eye Res. , vol.43 , pp. 383-396
    • Holmes, R.S.1    VandeBerg, J.L.2
  • 18
    • 0002431282 scopus 로고
    • Alcohol dehydrogenases and aldehyde dehydrogenases of anterior eye tissues from humans and other mammals
    • Kuriyama, K., Takada, A. and Ishii, H. (Eds.), Elsevier Science Publishers, Amsterdam
    • Holmes, R.S.: Alcohol dehydrogenases and aldehyde dehydrogenases of anterior eye tissues from humans and other mammals. In Kuriyama, K., Takada, A. and Ishii, H. (Eds.), Biomedical and Social Aspects of Alcohol and Alcoholism. Elsevier Science Publishers, Amsterdam (1988), pp 51-57.
    • (1988) Biomedical and Social Aspects of Alcohol and Alcoholism , pp. 51-57
    • Holmes, R.S.1
  • 19
    • 0024355688 scopus 로고
    • Isoelectric focusing studies of aldehyde dehydrogenases, alcohol dehydrogenases and oxidases from mammalian anterior eye tissues
    • Holmes, R.S., Cheung, B., and Vandeberg, J.L.: Isoelectric focusing studies of aldehyde dehydrogenases, alcohol dehydrogenases and oxidases from mammalian anterior eye tissues. Comp. Biochem. Physiol. 93B (1989). 271-277.
    • (1989) Comp. Biochem. Physiol. , vol.93 B , pp. 271-277
    • Holmes, R.S.1    Cheung, B.2    Vandeberg, J.L.3
  • 20
    • 0025819652 scopus 로고
    • Cloning and characterization of a new functional aldehyde dehydrogenase gene
    • Hsu, L.C. and Chang, W-C.: Cloning and characterization of a new functional aldehyde dehydrogenase gene. J. Biol. Chem. 266, (1991)12257-12265.
    • (1991) J. Biol. Chem. , vol.266 , pp. 12257-12265
    • Hsu, L.C.1    Chang, W.-C.2
  • 21
    • 0028566888 scopus 로고
    • Cloning of a cDNA encoding human ALDH7, a new member of the aldehyde dehydrogenase family
    • Hsu L.C., Chang W.-C. and Yoshida A.: Cloning of a cDNA encoding human ALDH7, a new member of the aldehyde dehydrogenase family. Gene 151 (1994) 285-289.
    • (1994) Gene , vol.151 , pp. 285-289
    • Hsu, L.C.1    Chang, W.-C.2    Yoshida, A.3
  • 22
    • 0024121572 scopus 로고
    • Cloning and complete nucleotide sequence of a full-length cDNA encoding a catalytically functional tumour-associated aldehyde dehydrogenase
    • Jones, D.E., Brennan, M.D., Hempel, J. and Lindahl, R.: Cloning and complete nucleotide sequence of a full-length cDNA encoding a catalytically functional tumour-associated aldehyde dehydrogenase. Proc. Natl. Acad. Sci. USA 85 (1988) 1782-1786.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 1782-1786
    • Jones, D.E.1    Brennan, M.D.2    Hempel, J.3    Lindahl, R.4
  • 23
    • 0015856911 scopus 로고
    • Light induced free radical oxidation of membrane lipid photoreceptors of frog retina
    • Kagan, V., Schvedova, A., Novikov, K and Kozlov, Y.: Light induced free radical oxidation of membrane lipid photoreceptors of frog retina.Biochem. Biophys. Acta 330 (1973) 76-79.
    • (1973) Biochem. Biophys. Acta , vol.330 , pp. 76-79
    • Kagan, V.1    Schvedova, A.2    Novikov, K.3    Kozlov, Y.4
  • 24
    • 0027521646 scopus 로고
    • Human corneal aldehyde dehydrogenase. Purification,kinetic characterization and phenotypic variation
    • King, G. and Holmes, R.: Human corneal aldehyde dehydrogenase. Purification,kinetic characterization and phenotypic variation. Biochem. and Mol. Biol. Int. 31 (1993) 49-63.
    • (1993) Biochem. and Mol. Biol. Int. , vol.31 , pp. 49-63
    • King, G.1    Holmes, R.2
  • 25
    • 0027131429 scopus 로고
    • Human aldehyde dehydrogenase cDNA cloning and primary structure of the enzyme that catalyzes dehydrogenation of 4-aminobutyraldehyde
    • Kurys, G., Shah, P.C., Kikonyogo, A., Reed, D., Ambroziak, W., and Pietruszko, R.: Human aldehyde dehydrogenase cDNA cloning and primary structure of the enzyme that catalyzes dehydrogenation of 4-aminobutyraldehyde. Eur. J. Biochem. 218 (1993) 311-320.
    • (1993) Eur. J. Biochem. , vol.218 , pp. 311-320
    • Kurys, G.1    Shah, P.C.2    Kikonyogo, A.3    Reed, D.4    Ambroziak, W.5    Pietruszko, R.6
  • 26
    • 0014949207 scopus 로고
    • Cleavage of structural protein during the assembly of the head of bacteriophage T4
    • Laemmli, U.K.: Cleavage of structural protein during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 30
    • 0023009193 scopus 로고
    • Increased sensitivity in peroxidase immunochemistry: A comparative study of a number of peroxidase visualisation methods employing a model system
    • Scopsi, L., Larsson, L.-I.: Increased sensitivity in peroxidase immunochemistry: A comparative study of a number of peroxidase visualisation methods employing a model system. J. Histochem. 84 (1986) 221-230.
    • (1986) J. Histochem. , vol.84 , pp. 221-230
    • Scopsi, L.1    Larsson, L.-I.2
  • 31
    • 0016713060 scopus 로고
    • Human liver aldehyde dehydrogenase esterase activity
    • Sidhu, R.S. and Blair, A.H.: Human liver aldehyde dehydrogenase esterase activity. J. Biol. Chem. 250 (1975) 7894-7898.
    • (1975) J. Biol. Chem. , vol.250 , pp. 7894-7898
    • Sidhu, R.S.1    Blair, A.H.2
  • 33
    • 0030032495 scopus 로고    scopus 로고
    • Lens crystallins of invertebrates: Diversity and recruitment from detoxification enzymes and novel proteins
    • Tomarev, S.I. and Piatigorsky, J.: Lens crystallins of invertebrates: diversity and recruitment from detoxification enzymes and novel proteins. Eur. J. Biochem. 235 (1996) 449-465.
    • (1996) Eur. J. Biochem. , vol.235 , pp. 449-465
    • Tomarev, S.I.1    Piatigorsky, J.2
  • 34
    • 0015216149 scopus 로고
    • Fluorescent glucosides in the human lens
    • van Heyningen, R.: Fluorescent glucosides in the human lens. Nature 230 (1970) 393-394.
    • (1970) Nature , vol.230 , pp. 393-394
    • Van Heyningen, R.1
  • 35
    • 0025885278 scopus 로고
    • Identification of bovine corneal protein 54 (BCP 54) as an aldehyde dehydrogenase
    • Verhagen, C., Hoekzema, R., Verjans, G.M.G.M. and Kijlstra, A.:Identification of bovine corneal protein 54 (BCP 54) as an aldehyde dehydrogenase. Exp. Eye Res. 53 (1991) 283-284.
    • (1991) Exp. Eye Res. , vol.53 , pp. 283-284
    • Verhagen, C.1    Hoekzema, R.2    Verjans, G.M.G.M.3    Kijlstra, A.4
  • 36
    • 0025890262 scopus 로고
    • Lens proteins expression in mammals: Taxon-specificity and the recruitment of crystallins
    • Wistow, G. and Kim, H.: Lens proteins expression in mammals: taxon-specificity and the recruitment of crystallins. J. Mol. Evol. 32 (1991) 262-269.
    • (1991) J. Mol. Evol. , vol.32 , pp. 262-269
    • Wistow, G.1    Kim, H.2
  • 37
    • 0020615817 scopus 로고
    • The role of sunlight in human cataract formation
    • Zigman S.: The role of sunlight in human cataract formation. Surv. Ophthalmol. 27 (1983) 317-326.
    • (1983) Surv. Ophthalmol. , vol.27 , pp. 317-326
    • Zigman, S.1
  • 38
    • 0002081151 scopus 로고
    • Photobiology of the lens
    • Maisel, H. (ed.), Marcel Dekker Inc.
    • Zigman, S.: Photobiology of the lens. In Maisel, H. (ed.), The Ocular Lens. Marcel Dekker Inc., 1985, pp301-347.
    • (1985) The Ocular Lens , pp. 301-347
    • Zigman, S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.