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1993 | 40 | 4 |
Tytuł artykułu

Nonidentity of subunits of human kidney arginase A1 and human liver arginase A5

Warianty tytułu
Języki publikacji
EN
Abstrakty
The main forms of arginase Ai from human kidney and As from human liver were purified to homogeneity. Molecular weight of both forms of enzyme approximates 120000. In the presence of EDTA these arginases dissociate into single type distinct subunits. Mr of both kinds of subunits is 30000. Similarly as native arginase forms, they differ in electric charge and display complete immunological incompatibility.
Wydawca
-
Rocznik
Tom
40
Numer
4
Opis fizyczny
p.465-470,fig.
Twórcy
autor
  • Medical Academy, S.Banacha 1, 02-097 Warsaw, Poland
autor
autor
autor
Bibliografia
  • 1. Hirsch-Kolb, H. & Greenberg, D.M. (1968) Molecular characteristics of rat liver arginase. /. Biol. Chem. 243,6123 - 6129.
  • 2. Carvajal, N., Martinez, J. & Fernandez, M. (1977) Immobilised monomer of human liver argi­nase. Biochim. Biophys. Acta 481,177 -183.
  • 3. Hosoyama, Y. (1972) The reversible inactivation of rat-liver arginase at low pH. Eur. }. Biochem. 27,48 - 52.
  • 4. Vielle-Breitburd, F. & Orth, G. (1972) Rabbit liver L-arginase purification, properties and subunit structure. J. Biol. Chem. 247,1227 -1255.
  • 5. Brusdeilins, M., Kuhner, R. & Schumacher, K. (1985) Purification, affinity to anti-human arginase immunoglobulin-Sepharose HB and subunit molecular weights of mammalian arginase. Biochim. Biophys. Acta 840,79 - 90.
  • 6. Pennicky, M., Simon, J.P. & Wiame, J.M. (1974) Interaction between arginase and L-ornithine carboyltransferase in Saccharomyces cerevisiae. Eur. J. Biochem. 49,429 - 442.
  • 7. Spector, E.B., Rice, S.C.H. & Cederbaum, S.D. (1983) Immunologic studies of arginase in tissues of normal human adult and arginase- -deficient patients. Pediat. Res. 17,941 - 944.
  • 8. Porembska, Z. & Zamecka, B. (1984) Immuno­logical properties of rat arginases. Acta Biochim. Pokm. 31,223 - 227.
  • 9. Zamecka, B. & Porembska, Z. (1988) Five forms of arginase in human tissues. Biochem. Med. Metabol. Biol. 39,258 - 266.
  • 10. Chinard, F.P, (1952) Photometric estimation of proline and ornithine. ]. Biol. Chem. 199,91 - 95.
  • 11. Lowry, O.H., Rosebrough, N.J., Farr, A.L. & Randall, R.J. (1951) Protein measurement with the Folin phenol reagent. J. Biol. Chem. 193, 265 -275.
  • 12. Warburg, O. & Christian, W. (1941) Isolierung und kristallisation des garungsfements enolase. Biochem. Z. 310,384 - 421.
  • 13. Andrews, P. (1964) Estimation of the molecular weight of proteins by Sephadex-gel filtration. Biochem. ]. 91,222 - 233.
  • 14. Skrzypek-Osiecka, I., Robin, Y. & Porembska, Z. (1983) Purification of rat kidney arginase Ai and A4 and their subcellular distribution. Acta Biochim. Polon. 30,83 - 92.15. Ber, E. & Muszyńska, G, (1979) Chemical modification of rat liver arginase. Acta Biochim. Polon. 26,103 - 114.
  • 16. Porembska, Z., Barańczyk, A. & Jachimowicz, J. (1971) Arginase isoenzymes in liver and kidney of some mammals. Acta Biochim. Polon. 16,77 - 85.
  • 17. Dizikes, G.J., Grody, W.W., Kern, R.M. & Cederbaum, S.D. (1985) Isolation and study of cDNA clones for human liver arginase. Am. J. Hum. Genet. 37,152 -154.
  • 18. Dizikes, G.J., Wayne, W.G., Kern, R.M. & Cederbaum, S.D. (1986) Isolation of human liver arginase cDNA and demonstration of non- homology between the two human arginase genes. Biochem. Biophys. Res. Commun. 141,53 - 59.
  • 19. Haraguchi, Y., Takiguchi, M., Amaya, Y., Kawamoto, I.M. & Mori, M. (1987) Molecular cloning and nucleotide sequence of cDNA for human liver arginase. Proc. Natl. Acad. Sci. U.S.A. 84,412 - 415.
  • 20. Ohtake, A., Takiguchi, M., Shigeto, Y., Amaya, Y., Kawamoto, S. & Mori, M. (1988) Structural organization of the gene for rat liver-type arginase. J. Biol. Chem. 263,2245 - 2249.
Typ dokumentu
Bibliografia
Identyfikatory
Identyfikator YADDA
bwmeta1.element.agro-article-f726a280-40d6-477e-b222-3f00ef3dbb98
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