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1994 | 41 | 1 |

Tytuł artykułu

AMP deaminase from anterior lobe of bovine pituitary: purification and properties

Warianty tytułu

Języki publikacji

EN

Abstrakty

EN
AMP deaminase (EC 3.5.4.6) from anterior lobe of bovine pituitary has been purified for the first time. Six molecular forms of the enzyme were eluted from phosphocellulose Pll with a KC1 concentration gradient. By two stage gel chromatography individual molecular forms were purified to electrophoretic homogeneity. Comparison of some physico-chemical and kinetic properties of the preparations obtained showed high similarity of their properties to those of AMP deaminase from other animal tissues already described. All the isoforms were found to be Zn2+-dependent.

Wydawca

-

Rocznik

Tom

41

Numer

1

Opis fizyczny

p.97-101,fig.

Twórcy

autor
  • Institute of Biochemistry of Armenian Academy of Sciences, B.Sevag 5/1, 375044 Yerevan, Armenia
autor

Bibliografia

  • 1. Ogasawara, N.,Goto, H.,Yamada,Y., Watanabe, T. & Asa no, T. (1982) AMP deaminase isozymes in human tissues. Biochim. Biophys. Acta 714, 298-306.
  • 2. Ogasawara, N., Goto, H., Watanabe, T., Kawamura, Y. & Yoshino, M. (1974) Multiple forms of AMP deaminase in various rat tissues. FEBS Lett. 44,63-66.
  • 3. Ogasawara, N., Goto, H. & Watanabe, T. (1975) Isozymes of rat brain AMP deaminase: developmental changes and characterizations of five forms. FEBS Lett. 58,245-248.
  • 4. Ogasawara, N., Goto, H. & Watanabe, T. (1975) Isozymes of rat AMP deaminase. Biochim. Biophys. Acta 403,530-537.
  • 5. Haroutunian, A. & Lowenstein, J. (1977) Multiple forms of rat brain AMP deaminase. Doklady Akademii Nauk S.S.S.R. 234,951-954.
  • 6. Setlow, B. & Lowenstein, J. (1967) Adenylate deaminase. II. Purification and some regulatory properties of the enzyme from calf brain. J. Biot. Chem. 242,607-615.
  • 7. Rhoads, D. (1969) Studies on adenylate deaminase from calf brain. Ph.D. Thesis, Brandeis University.
  • 8. Sharoyan, S., Mardanian, S. & Haroutunian, A. (1992) Isolation of AMP deaminase molecular forms from the cattle nerve tissue. Neurokhimiya 11,158-165.9. Sugawara, K. & Oyama, F. (1981) Fluorogenic reaction and specific microdetermination of ammonia. /. Biochcm. (Tokyo) 89,771-774.
  • 10. Bradford, M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Ajial. Biochem. 72,248-254.
  • 11. Weber, K. & Osbom, M. (1969) The reliability of molecular weigh determinations by dodccyl sulfate-polyacrylamide gel electrophoresis. /. Biol. Chem. 244,4406^412.
  • 12. Dixon, M. (1953) The determination of enzyme inhibitor constants. Biochem. J. 55,170-171.
  • 13. Setlow, B. & Lowenstein, J. (1968) Adenylate deaminase. IV. Nucleotide specificity of the enzyme from calf brain with special reference to guanosine triphosphate. /. Biol. Chem. 243, 3409-3415.
  • 14. Setlow, B. & Lowenstein, J. (1968) Adenylate deaminase. V. Effect of alkali metal and magnesium ions on activity. /. Biol. Chem. 243, 6216-6221.
  • 15. Haroutunian, A. (1974) AMP-aminohydrolasc of brain and other organs and the regulation of its activity. Problems of Brain Biochemistry (in Russian) 9,251-272.
  • 16. Raggi, A., Ranieri, M., Taponeco, G., Ronca-Testoni, S., Ronca, G. & Rossi, C. (1970) Interaction of rat muscle AMP aminohydrolase with chelating agents and metal ions. FEBS Lett. 10,101-104.
  • 17. Zielke, C. & Suelter, C. (1971) Rabbit muscle adenosine 5'-monophosphate aminohydrolase. Characterization as a zinc metalloenzyme. /. Biol. Chem. 246,2179-2186.
  • 18. Makarewicz, W. (1974) Purification and pro­perties of AMP-aminohydrolase from human placenta. Acta Biochim. Polon. 21,125-135.
  • 19. Stankiewicz, A. & Makarewicz, W. (1975) AMP deaminase of human skeletal muscle. Divalent metal cations and catalytic activity. Biochem. Medicine 13,197-212.
  • 20. Stankiewicz, A., Spychała, J., Składanowski, A. & Źydowo, M. (1979) Comparative studies on muscle AMP deaminase. I. Purification, mol­ecular weight, subunit structure and metal content of the enzymes from rat, rabbit, hen, frog and pikeperch. Camp. Biochem. Physiol. 62B, 363-369.
  • 21. Ito, K., Yamamoto, H. & Mizugaki, M. (1988) Purification and general properties of AMP deaminase from sheep brain. /. Biochem. (Tokyo) 103,259-262.

Typ dokumentu

Bibliografia

Identyfikatory

Identyfikator YADDA

bwmeta1.element.agro-article-4c5f3f68-4ed5-450c-97f1-b78ab1679d2c
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