메뉴 건너뛰기




Volumn 262, Issue 1-2, 2004, Pages 119-126

AMP-deaminase from normal and cirrhotic human liver: A comparative study

Author keywords

Acoholic liver cirrhosis; Human liver AMP deaminase

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE MONOPHOSPHATE DEAMINASE; ADENOSINE PHOSPHATE; ADENOSINE TRIPHOSPHATE; DODECYL SULFATE SODIUM; GUANOSINE TRIPHOSPHATE; PHOSPHATE;

EID: 4344625876     PISSN: 03008177     EISSN: None     Source Type: Journal    
DOI: 10.1023/B:MCBI.0000038217.71621.88     Document Type: Article
Times cited : (4)

References (31)
  • 1
    • 0014664040 scopus 로고
    • Purification and properties of rat liver AMP deaminase
    • Smith LD, Kizer DE: Purification and properties of rat liver AMP deaminase. Biochim Biophys Acta 191: 415-424, 1969
    • (1969) Biochim. Biophys. Acta , vol.191 , pp. 415-424
    • Smith, L.D.1    Kizer, D.E.2
  • 2
    • 0014944185 scopus 로고
    • Muscle AMP aminohydrolase. III. A comparative study on the regulatory properties of skeletal muscle enzyme from various species
    • Ronca-Testoni S, Raggi A, Ronca G: Muscle AMP aminohydrolase. III. A comparative study on the regulatory properties of skeletal muscle enzyme from various species. Biochim Biophys Acta 198: 101-112, 1970
    • (1970) Biochim. Biophys. Acta , vol.198 , pp. 101-112
    • Ronca-Testoni, S.1    Raggi, A.2    Ronca, G.3
  • 3
    • 0018276297 scopus 로고
    • Human erythrocyte 5′-AMP aminohydrolase. Purification and characterization
    • Yun S, Suelter CH: Human erythrocyte 5′-AMP aminohydrolase. Purification and characterization. J Biol Chem 253: 404-408, 1978
    • (1978) J. Biol. Chem. , vol.253 , pp. 404-408
    • Yun, S.1    Suelter, C.H.2
  • 4
    • 0018765025 scopus 로고
    • Regulatory properties of rat heart AMP deaminase
    • Kaletha K, Skladanowski A: Regulatory properties of rat heart AMP deaminase. Biochim Biophys Acta 568: 80-90, 1979
    • (1979) Biochim. Biophys. Acta , vol.568 , pp. 80-90
    • Kaletha, K.1    Skladanowski, A.2
  • 5
    • 0015738302 scopus 로고
    • Stabilization of the adenylate energy charge by the adenylate deaminase reaction
    • Chapman AG, Atkinson DE: Stabilization of the adenylate energy charge by the adenylate deaminase reaction. J Biol Chem 248: 8309-8312, 1973
    • (1973) J. Biol. Chem. , vol.248 , pp. 8309-8312
    • Chapman, A.G.1    Atkinson, D.E.2
  • 6
    • 0017328813 scopus 로고
    • The mechanism of adenosine triphosphate depletion in the liver after a load of fructose
    • Van den Berghe G, Bronfman M, Vanneste R, Hers H: The mechanism of adenosine triphosphate depletion in the liver after a load of fructose. Biochem J 162: 601-609, 1977
    • (1977) Biochem. J. , vol.162 , pp. 601-609
    • Van den Berghe, G.1    Bronfman, M.2    Vanneste, R.3    Hers, H.4
  • 8
    • 0023851957 scopus 로고
    • Developmental forms of human skeletal-muscle AMP deaminase. The kinetic and regulatory properties of the enzyme
    • Kaletha K, Nowak G: Developmental forms of human skeletal-muscle AMP deaminase. The kinetic and regulatory properties of the enzyme. Biochem J 249: 255-261, 1987
    • (1987) Biochem. J. , vol.249 , pp. 255-261
    • Kaletha, K.1    Nowak, G.2
  • 9
    • 0006648317 scopus 로고
    • Evidence for sequential expression of multiple AMP deaminase isoforms during skeletal muscle development
    • Marquetant R, Desai NM, Sabina RL, Holmes EW: Evidence for sequential expression of multiple AMP deaminase isoforms during skeletal muscle development. Proc Natl Acad Sci USA 84: 2345-2349, 1987
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 2345-2349
    • Marquetant, R.1    Desai, N.M.2    Sabina, R.L.3    Holmes, E.W.4
  • 11
    • 0025310830 scopus 로고
    • Adenylate deaminase. A multigene family in humans and rats
    • Morisaki T, Sabina RL, Holmes EW: Adenylate deaminase. A multigene family in humans and rats. J Biol Chem 265: 11482-11486, 1990
    • (1990) J. Biol. Chem. , vol.265 , pp. 11482-11486
    • Morisaki, T.1    Sabina, R.L.2    Holmes, E.W.3
  • 12
    • 0026564429 scopus 로고
    • Molecular cloning of AMP deaminase isoform L. Sequence and bacterial expression of human AMPD2 cDNA
    • Bausch-Jurken MT, Mahnke-Zizelman DK, Morisaki T, Sabina RL: Molecular cloning of AMP deaminase isoform L. Sequence and bacterial expression of human AMPD2 cDNA. J Biol Chem 267: 22407-22413, 1992
    • (1992) J. Biol. Chem. , vol.267 , pp. 22407-22413
    • Bausch-Jurken, M.T.1    Mahnke-Zizelman, D.K.2    Morisaki, T.3    Sabina, R.L.4
  • 13
    • 0026726662 scopus 로고
    • Cloning of human AMP deaminase isoform E cDNAs. Evidence for a third AMPD gene exhibiting alternatively spliced 5′-exons
    • Mahnke-Zizelman DK, Sabina RL: Cloning of human AMP deaminase isoform E cDNAs. Evidence for a third AMPD gene exhibiting alternatively spliced 5′-exons. J Biol Chem 267: 20866-20877, 1992
    • (1992) J. Biol. Chem. , vol.267 , pp. 20866-20877
    • Mahnke-Zizelman, D.K.1    Sabina, R.L.2
  • 14
    • 0029591590 scopus 로고
    • Characterization of human AMP deaminase 2 (AMPD2) gene expression reveals alternative transcripts encoding variable N-terminal extension of isoform L
    • Van den Berghe F, Sabina RL: Characterization of human AMP deaminase 2 (AMPD2) gene expression reveals alternative transcripts encoding variable N-terminal extension of isoform L. Biochem J 312: 401-410, 1995
    • (1995) Biochem. J. , vol.312 , pp. 401-410
    • Van den Berghe, F.1    Sabina, R.L.2
  • 15
    • 0019053620 scopus 로고
    • Effects of storage on activity and subunit structure of rabbit skeletal muscle AMP deaminase
    • Ranieri-Raggi M, Raggi A: Effects of storage on activity and subunit structure of rabbit skeletal muscle AMP deaminase. Biochem J 189: 367-368, 1980
    • (1980) Biochem. J. , vol.189 , pp. 367-368
    • Ranieri-Raggi, M.1    Raggi, A.2
  • 16
    • 0032567534 scopus 로고    scopus 로고
    • Novel aspects of tetramer assembly and N-terminal domain structure and function are revealed by recombinant expression of human AMP deaminase isoforms
    • Mahnke-Zizelman DK, Tullson PC, Sabina RL: Novel aspects of tetramer assembly and N-terminal domain structure and function are revealed by recombinant expression of human AMP deaminase isoforms. J Biol Chem 273: 35118-35125, 1998
    • (1998) J. Biol. Chem. , vol.273 , pp. 35118-35125
    • Mahnke-Zizelman, D.K.1    Tullson, P.C.2    Sabina, R.L.3
  • 17
    • 0033802601 scopus 로고    scopus 로고
    • Towards an understanding of the functional significance of N-terminal domain divergence in human AMP deaminase isoforms
    • Sabina RL, Mahnke-Zizelman DK: Towards an understanding of the functional significance of N-terminal domain divergence in human AMP deaminase isoforms. Pharmacol Ther 87: 279-283, 2000
    • (2000) Pharmacol. Ther. , vol.87 , pp. 279-283
    • Sabina, R.L.1    Mahnke-Zizelman, D.K.2
  • 18
    • 0037297179 scopus 로고    scopus 로고
    • Expression, purification, and inhibition in vitro proteolysis of human AMPD2 (isoform L) recombinant enzymes
    • Haas A, Sabina RL: Expression, purification, and inhibition in vitro proteolysis of human AMPD2 (isoform L) recombinant enzymes. Protein Expr Purif 27: 293-303, 2003
    • (2003) Protein Expr. Purif. , vol.27 , pp. 293-303
    • Haas, A.1    Sabina, R.L.2
  • 20
    • 0014216746 scopus 로고
    • An improved purification, crystallization, and some properties of rabbit muscle 5′-adenylic acid deaminase
    • Smiley KL, Berry AJ, Suelter CH: An improved purification, crystallization, and some properties of rabbit muscle 5′-adenylic acid deaminase. J Biol Chem 242: 2502-2506, 1967
    • (1967) J. Biol. Chem. , vol.242 , pp. 2502-2506
    • Smiley, K.L.1    Berry, A.J.2    Suelter, C.H.3
  • 21
    • 0025863101 scopus 로고
    • Purification and properties of AMP-deaminase from human uterine smooth muscle
    • Nagel-Starczynowska G, Nowak G, Kaletha K: Purification and properties of AMP-deaminase from human uterine smooth muscle. Biochim Biophys Acta 1073: 470-473, 1991
    • (1991) Biochim. Biophys. Acta , vol.1073 , pp. 470-473
    • Nagel-Starczynowska, G.1    Nowak, G.2    Kaletha, K.3
  • 22
    • 33646400526 scopus 로고
    • Modified reagents for determination of urea and ammonia
    • Chaney AL, Marbach EP: Modified reagents for determination of urea and ammonia. Clin Chem 8: 130-132, 1961
    • (1961) Clin. Chem. , vol.8 , pp. 130-132
    • Chaney, A.L.1    Marbach, E.P.2
  • 23
    • 0025765340 scopus 로고
    • Purification and properties of AMP-deaminase from human uterine smooth muscle. Regulation by adenylate energy charge and activated fatty acids
    • Nowak G, Nagel-Starczynowska G, Kaletha K: Purification and properties of AMP-deaminase from human uterine smooth muscle. Regulation by adenylate energy charge and activated fatty acids. Biochim Biophys Acta 1078: 303-304, 1991
    • (1991) Biochim. Biophys. Acta , vol.1078 , pp. 303-304
    • Nowak, G.1    Nagel-Starczynowska, G.2    Kaletha, K.3
  • 24
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein using the principle of protein-dye binding
    • Bradford MM: A rapid and sensitive method for the quantitation of microgram quantities of protein using the principle of protein-dye binding. Anal Biochem 72: 248-254, 1976
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 25
    • 0002840661 scopus 로고
    • Use of blotted proteins as immunogenes
    • B. Dunbar (ed.). IRL Press, Oxford
    • Szewczyk B, Harper DR: Use of blotted proteins as immunogenes. In: B. Dunbar (ed.). Protein Blotting. A Practical Approach. IRL Press, Oxford, 1994, pp 189-205
    • (1994) Protein Blotting. A Practical Approach , pp. 189-205
    • Szewczyk, B.1    Harper, D.R.2
  • 26
    • 0026628769 scopus 로고
    • Purification and properties of AMP-deaminase from human kidney
    • Nowak G, Kaletha K: Purification and properties of AMP-deaminase from human kidney. Biochem Med Metab Biol 47: 232-241, 1992
    • (1992) Biochem. Med. Metab. Biol. , vol.47 , pp. 232-241
    • Nowak, G.1    Kaletha, K.2
  • 28
    • 0021174629 scopus 로고
    • Ethanol-induced activation of adenine nucleotide turnover. Evidence for a role of acetate
    • Puig JG, Fox IH: Ethanol-induced activation of adenine nucleotide turnover. evidence for a role of acetate. J Clin Invest 74: 936-941, 1984
    • (1984) J. Clin. Invest. , vol.74 , pp. 936-941
    • Puig, J.G.1    Fox, I.H.2
  • 29
    • 0028345807 scopus 로고
    • Clinical and biochemical aspects of uric acid over-production
    • Puig JG, Mateos FA: Clinical and biochemical aspects of uric acid over-production. Pharm World Sci 16: 40-54, 1994
    • (1994) Pharm. World Sci. , vol.16 , pp. 40-54
    • Puig, J.G.1    Mateos, F.A.2
  • 30
    • 0004266917 scopus 로고
    • 2nd edn. Lippincott, Philadelphia
    • Rubin E, Farber JL: In: Pathology, 2nd edn. Lippincott, Philadelphia, 1994, p 740
    • (1994) Pathology , pp. 740
    • Rubin, E.1    Farber, J.L.2
  • 31
    • 0017287004 scopus 로고
    • Role of the adenylate deaminase reaction in regulation of adenine nucleotide metabolism in ehrlich ascites tumor
    • Chapman AG, Miller AL, Atkinson DE: Role of the adenylate deaminase reaction in regulation of adenine nucleotide metabolism in ehrlich ascites tumor. Cells Cancer Res 36: 1144-1150, 1976
    • (1976) Cells Cancer Res. , vol.36 , pp. 1144-1150
    • Chapman, A.G.1    Miller, A.L.2    Atkinson, D.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.