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Volumn 17, Issue 3, 1998, Pages 205-212

Prolyl hydroxylase activity in tissue homogenates of annelids from deep sea hydrothermal vents

Author keywords

Alvinella; Deep sea hydrothermal vents; Prolyl 4 hydroxylase

Indexed keywords

2 OXOGLUTARIC ACID; 2,2' BIPYRIDINE; ASCORBIC ACID; ENZYME INHIBITOR; FERROUS ION; OXYGEN; PROCOLLAGEN; PROCOLLAGEN PROLINE 2 OXOGLUTARATE 4 DIOXYGENASE; PROTOCATECHUIC ACID; SYNTHETIC PEPTIDE; WATER;

EID: 0031879608     PISSN: 0945053X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0945-053X(98)90059-2     Document Type: Article
Times cited : (12)

References (28)
  • 2
    • 0020016034 scopus 로고
    • Determination of 3- and 4-hydroxyproline
    • Berg, R.A.: Determination of 3- and 4-hydroxyproline. Meth. Enzymol. 82: 372-398, 1982.
    • (1982) Meth. Enzymol. , vol.82 , pp. 372-398
    • Berg, R.A.1
  • 3
    • 0015624009 scopus 로고
    • The thermal transition of a non-hydroxylated form of collagen. Evidence for a role for hydroxyproline in stabilizing the triple-helix of collagen
    • Berg, R.A. and Prockop, D.J.: The thermal transition of a non-hydroxylated form of collagen. Evidence for a role for hydroxyproline in stabilizing the triple-helix of collagen. Biochem. Biophys. Res. Commun. 52: 115-120, 1973.
    • (1973) Biochem. Biophys. Res. Commun. , vol.52 , pp. 115-120
    • Berg, R.A.1    Prockop, D.J.2
  • 4
    • 0032484948 scopus 로고    scopus 로고
    • Worms bask in extreme temperatures
    • Cary, S.C., Shank, T. and Stein, J.: Worms bask in extreme temperatures. Nature 391: 545-546, 1998.
    • (1998) Nature , vol.391 , pp. 545-546
    • Cary, S.C.1    Shank, T.2    Stein, J.3
  • 6
    • 0027068701 scopus 로고
    • The biology of hydrothermal vent animals: Physiology, biochemistry and autotrophic symbioses
    • Childress, J.J. and Fisher, C.R.: The biology of hydrothermal vent animals: physiology, biochemistry and autotrophic symbioses. Oceanogr. Mar. Biol. Ann. Rev. 230: 337-441, 1992.
    • (1992) Oceanogr. Mar. Biol. Ann. Rev. , vol.230 , pp. 337-441
    • Childress, J.J.1    Fisher, C.R.2
  • 9
    • 0014669264 scopus 로고
    • Protocollagen proline hydroxylase from Ascaris lumbricoides
    • Fujimoto, D. and Prockop, D.J.: Protocollagen proline hydroxylase from Ascaris lumbricoides. J. Biol. Chem. 244: 205-210, 1969.
    • (1969) J. Biol. Chem. , vol.244 , pp. 205-210
    • Fujimoto, D.1    Prockop, D.J.2
  • 10
    • 0027469958 scopus 로고
    • Aspects of life development at deep sea hydrothermal vents
    • Gaill, F.: Aspects of life development at deep sea hydrothermal vents. FASEB J. 7: 558-565, 1993.
    • (1993) FASEB J. , vol.7 , pp. 558-565
    • Gaill, F.1
  • 11
    • 0000699597 scopus 로고
    • The biology of annelid worms from high temperature hydrothermal vent regions
    • Gaill, F. and Hunt, S.: The biology of annelid worms from high temperature hydrothermal vent regions. Rev. Aquat. Sci. 4: 107-137, 1991.
    • (1991) Rev. Aquat. Sci. , vol.4 , pp. 107-137
    • Gaill, F.1    Hunt, S.2
  • 12
    • 0028946046 scopus 로고
    • Structural comparison of cuticle and interstitial collagens from annelids living in shallow sea water and at deep-sea hydrothermal vents
    • Gaill, E, Mann, K.H., Wiedemann, H., Engel, J. and Timpl, R.: Structural comparison of cuticle and interstitial collagens from annelids living in shallow sea water and at deep-sea hydrothermal vents. J. Mol. Biol. 246: 284-294, 1995.
    • (1995) J. Mol. Biol. , vol.246 , pp. 284-294
    • Gaill, E.1    Mann, K.H.2    Wiedemann, H.3    Engel, J.4    Timpl, R.5
  • 13
    • 0025879008 scopus 로고
    • Characterization of two forms of collagen from worms collected at deep-sea level
    • Gaill, F., Wiedemann, H., Mann, K., Kühn, K., Timpl, R. and Engel, J.: Characterization of two forms of collagen from worms collected at deep-sea level. J. Mol. Biol. 221: 209-223, 1991.
    • (1991) J. Mol. Biol. , vol.221 , pp. 209-223
    • Gaill, F.1    Wiedemann, H.2    Mann, K.3    Kühn, K.4    Timpl, R.5    Engel, J.6
  • 14
    • 0024259872 scopus 로고
    • Syncatalytic inactivation of prolyl 4-hydroxylase by synthetic peptides containing the unphysiologic amino acid 5-oxaproline
    • Günzler, V., Brocks, D., Henke, S., Myllylä, R., Geiger, R. and Kivirikko, K.I.: Syncatalytic inactivation of prolyl 4-hydroxylase by synthetic peptides containing the unphysiologic amino acid 5-oxaproline. J. Biol. Chem. 263: 19498-19504, 1988.
    • (1988) J. Biol. Chem. , vol.263 , pp. 19498-19504
    • Günzler, V.1    Brocks, D.2    Henke, S.3    Myllylä, R.4    Geiger, R.5    Kivirikko, K.I.6
  • 15
    • 0001312106 scopus 로고
    • Cofactor and cosubstrate requirements of collagen proline hydroxylase
    • Hutton, J.J., Tappel, A.L. and Udenfriend, S.: Cofactor and cosubstrate requirements of collagen proline hydroxylase. Arch. Biochem. Biophys. 118: 231-240, 1967.
    • (1967) Arch. Biochem. Biophys. , vol.118 , pp. 231-240
    • Hutton, J.J.1    Tappel, A.L.2    Udenfriend, S.3
  • 16
    • 0025122004 scopus 로고
    • 14C]succinate: Application to prolyl 4-hydroxylase
    • 14C]succinate: Application to prolyl 4-hydroxylase. Anal. Biochem. 184: 291-297, 1990.
    • (1990) Anal. Biochem. , vol.184 , pp. 291-297
    • Kaule, G.1    Günzler, V.2
  • 17
    • 0019593706 scopus 로고
    • An improved method for the purification of vertebrate prolyl hydroxylase by affinity chromatography
    • Kedersha, N.L. and Berg, R.A.: An improved method for the purification of vertebrate prolyl hydroxylase by affinity chromatography. Collagen Rel. Res. 1: 345-353, 1981.
    • (1981) Collagen Rel. Res. , vol.1 , pp. 345-353
    • Kedersha, N.L.1    Berg, R.A.2
  • 18
    • 0020010503 scopus 로고
    • Posttranslational enzymes in the biosynthesis of collagen: Intracellular enzymes
    • Kivirikko, K.I. and Myllylä, R.: Posttranslational enzymes in the biosynthesis of collagen: intracellular enzymes. Meth. Enzymol. 82: 245-304, 1982.
    • (1982) Meth. Enzymol. , vol.82 , pp. 245-304
    • Kivirikko, K.I.1    Myllylä, R.2
  • 19
    • 0023021512 scopus 로고
    • Partial identity of the 2-oxoglutarate and ascorbate binding sites of prolyl 4-hydroxylase
    • Majamaa, K., Günzler, V., Hanauske-Abel, H.M., Myllylä, R. and Kivirikko, K.I.: Partial identity of the 2-oxoglutarate and ascorbate binding sites of prolyl 4-hydroxylase. J. Biol. Chem. 261: 7819-7823, 1986.
    • (1986) J. Biol. Chem. , vol.261 , pp. 7819-7823
    • Majamaa, K.1    Günzler, V.2    Hanauske-Abel, H.M.3    Myllylä, R.4    Kivirikko, K.I.5
  • 20
    • 0021765030 scopus 로고
    • The 2-oxoglutarate binding site of prolyl 4-hydroxylase. Identification of distinct subsites and evidence for 2-oxoglutarate decarboxylation in a ligand reaction at the enzyme-bound ferrous ion
    • Majamaa, K., Hanauske-Abel, H.M., Günzler, V. and Kivirikko, K.I.: The 2-oxoglutarate binding site of prolyl 4-hydroxylase. Identification of distinct subsites and evidence for 2-oxoglutarate decarboxylation in a ligand reaction at the enzyme-bound ferrous ion. Eur. J. Biochem. 138: 239-245, 1984.
    • (1984) Eur. J. Biochem. , vol.138 , pp. 239-245
    • Majamaa, K.1    Hanauske-Abel, H.M.2    Günzler, V.3    Kivirikko, K.I.4
  • 21
    • 0027097977 scopus 로고
    • Amino-acid sequence and cell-adhesion activity of a fibril-forming collagen from the tube worm Riftia pachyptila living at deep sea hydrothermal vents
    • Mann, K., Gaill, F. and Timpl, R.: Amino-acid sequence and cell-adhesion activity of a fibril-forming collagen from the tube worm Riftia pachyptila living at deep sea hydrothermal vents. Eur. J. Biochem. 210: 839-847, 1992.
    • (1992) Eur. J. Biochem. , vol.210 , pp. 839-847
    • Mann, K.1    Gaill, F.2    Timpl, R.3
  • 22
    • 0017742181 scopus 로고
    • Mechanism of the prolyl hydroxylase reaction. 2. Kinetic analysis of the reaction sequence
    • Myllylä, R., Tuderman, L. and Kivirikko, K.I.: Mechanism of the prolyl hydroxylase reaction. 2. Kinetic analysis of the reaction sequence. Eur. J. Biochem. 80: 349-357, 1977.
    • (1977) Eur. J. Biochem. , vol.80 , pp. 349-357
    • Myllylä, R.1    Tuderman, L.2    Kivirikko, K.I.3
  • 23
    • 0016862346 scopus 로고
    • Modification of the tritium-release assays for prolyl and lysyl hydroxylases using Dowex-50 columns
    • Peterkofsky, B. and DiBlasio, R.: Modification of the tritium-release assays for prolyl and lysyl hydroxylases using Dowex-50 columns. Anal. Biochem. 66: 279-286, 1975.
    • (1975) Anal. Biochem. , vol.66 , pp. 279-286
    • Peterkofsky, B.1    DiBlasio, R.2
  • 24
    • 0016267847 scopus 로고
    • Activities of prolyl hydroxylase, lysyl hydroxylase, collagen galactosyltransferase and collagen glucosyltransferase in the liver of rats with hepatic injury
    • Risteli, J. and Kivirikko, K.I.: Activities of prolyl hydroxylase, lysyl hydroxylase, collagen galactosyltransferase and collagen glucosyltransferase in the liver of rats with hepatic injury. Biochem. J. 144: 115-122, 1974.
    • (1974) Biochem. J. , vol.144 , pp. 115-122
    • Risteli, J.1    Kivirikko, K.I.2
  • 25
    • 13144270147 scopus 로고
    • Transport, metabolism and detoxification of hydrogen sulfide in animals from sulfide-rich environments
    • Somero, G.N., Childress, J.J. and Anderson, A.E.: Transport, metabolism and detoxification of hydrogen sulfide in animals from sulfide-rich environments. Rev. Aquat. Sci. 2: 399-436, 1989.
    • (1989) Rev. Aquat. Sci. , vol.2 , pp. 399-436
    • Somero, G.N.1    Childress, J.J.2    Anderson, A.E.3
  • 26
    • 0026365390 scopus 로고
    • The biology of hydrothermal vent animals: Ecology and evolution
    • Tunnicliffe, V.: The biology of hydrothermal vent animals: ecology and evolution. Oceanogr. Mar. Biol. Ann. Rev. 29: 319-407, 1991.
    • (1991) Oceanogr. Mar. Biol. Ann. Rev. , vol.29 , pp. 319-407
    • Tunnicliffe, V.1
  • 27
    • 0016593798 scopus 로고
    • An affinity-column procedure using poly (L-proline) for the purification of prolyl hydroxylase. Purification of the enzyme from chick embryos
    • Tuderman, L., Kuutti, E.R. and Kivirikko, K.I.: An affinity-column procedure using poly (L-proline) for the purification of prolyl hydroxylase. Purification of the enzyme from chick embryos. Eur. J. Biochem. 25: 9-16, 1975.
    • (1975) Eur. J. Biochem. , vol.25 , pp. 9-16
    • Tuderman, L.1    Kuutti, E.R.2    Kivirikko, K.I.3
  • 28
    • 0017697003 scopus 로고
    • Mechanism of the prolyl hydroxylase reaction: 1. Role of co-substrates
    • Tuderman, L., Myllylä, R. and Kivirikko, K.L: Mechanism of the prolyl hydroxylase reaction: 1. Role of co-substrates. Eur. J. Biochem. 80: 341-348, 1977.
    • (1977) Eur. J. Biochem. , vol.80 , pp. 341-348
    • Tuderman, L.1    Myllylä, R.2    Kivirikko, K.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.