Skip to main content
Biochemical Journal logoLink to Biochemical Journal
. 1974 Dec;143(3):591–597. doi: 10.1042/bj1430591

Structure and properties of arginase from the polychaete annelid Pista pacifica Berkeley

Karen L O'Malley 1, Robert C Terwilliger 1
PMCID: PMC1168428  PMID: 4462743

Abstract

An oligomeric arginase with a molecular weight of 205000 is present in the intestinal tissues of the polychaete annelid Pista pacifica. The presence of an active subunit with a molecular weight of 34000 was demonstrated. The enzyme specificity, effect of thiol reagents on activity, kinetic properties of the intact enzyme and the active subunit were investigated. Treatment of the arginase with EDTA results in its dissociation into an inactive subunit; the active oligomeric structure can be regenerated by addition of Mn2+. The correlation of characteristics of arginase from a certain species and that species, mode of nitrotelism is discussed.

Full text

PDF
591

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Andrews P. The gel-filtration behaviour of proteins related to their molecular weights over a wide range. Biochem J. 1965 Sep;96(3):595–606. doi: 10.1042/bj0960595. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Baret R., Girard C., Riou J. Sur certaines propriétés des arginases du tissu hépatopancréatiqe d'Helix pomatia lin. et d'Helix aspersa müll. Biochimie. 1972;54(4):421–430. doi: 10.1016/s0300-9084(72)80225-6. [DOI] [PubMed] [Google Scholar]
  3. Bascur L., Cabello J., Véliz M., González A. Molecular forms of human-liver arginase. Biochim Biophys Acta. 1966 Oct 17;128(1):149–154. doi: 10.1016/0926-6593(66)90151-2. [DOI] [PubMed] [Google Scholar]
  4. Brown G. W., Jr Studies in comparative biochemistry and evolution. I. Avian liver arginase. Arch Biochem Biophys. 1966 Apr;114(1):184–194. doi: 10.1016/0003-9861(66)90320-1. [DOI] [PubMed] [Google Scholar]
  5. Campbell J. W. A comparative study of molluscan and mammalian arginases. Comp Biochem Physiol. 1966 May;18(1):179–199. doi: 10.1016/0010-406x(66)90343-4. [DOI] [PubMed] [Google Scholar]
  6. Carlisky N. J., Sadnik I. L. Properties of amphibian renal arginase. I. The effect of dialysis and sulphydryl compounds. Comp Biochem Physiol B. 1972 Apr 15;41(4):785–792. doi: 10.1016/0305-0491(72)90091-0. [DOI] [PubMed] [Google Scholar]
  7. Carvajal N., Venegas A., Oestreicher G., Plaza M. Effect of manganese on the quaternary structure of human liver arginase. Biochim Biophys Acta. 1971 Nov 13;250(2):437–442. doi: 10.1016/0005-2744(71)90200-2. [DOI] [PubMed] [Google Scholar]
  8. Cvancara V. A. Liver arginase activity in the sockeye salmon, Oncorhynchus nerka. Comp Biochem Physiol B. 1971 Nov 15;40(3):819–822. doi: 10.1016/0305-0491(71)90156-8. [DOI] [PubMed] [Google Scholar]
  9. DAVIS B. J. DISC ELECTROPHORESIS. II. METHOD AND APPLICATION TO HUMAN SERUM PROTEINS. Ann N Y Acad Sci. 1964 Dec 28;121:404–427. doi: 10.1111/j.1749-6632.1964.tb14213.x. [DOI] [PubMed] [Google Scholar]
  10. Hartenstein R. Characteristics of arginase from the freshwater crayfish, Cambarus bartoni. Comp Biochem Physiol B. 1971 Nov 15;40(3):781–795. doi: 10.1016/0305-0491(71)90152-0. [DOI] [PubMed] [Google Scholar]
  11. Hirsch-Kolb H., Greenberg D. M. Molecular characteristics of rat liver arginase. J Biol Chem. 1968 Dec 10;243(23):6123–6129. [PubMed] [Google Scholar]
  12. Hirsch-Kolb H., Heine J. P., Kolb H. J., Greenberg D. M. Comparative physical-chemical studies of mammalian arginases. Comp Biochem Physiol. 1970 Dec 1;37(3):345–359. doi: 10.1016/0010-406x(70)90563-3. [DOI] [PubMed] [Google Scholar]
  13. Hirsch-Kolb H., Kolb H. J., Greenberg D. M. Nuclear magnetic resonance studies of manganese binding of rat liver arginase. J Biol Chem. 1971 Jan 25;246(2):395–401. [PubMed] [Google Scholar]
  14. LINN S., LEHMAN I. R. AN ENDONUCLEASE FROM NEUROSPORA CRASSA SPECIFIC FOR POLYNUCLEOTIDES LACKING AN ORDERED STRUCTURE. I. PURIFICATION AND PROPERTIES OF THE ENZYME. J Biol Chem. 1965 Mar;240:1287–1293. [PubMed] [Google Scholar]
  15. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  16. Mora J., Tarrab R., Bojalil L. F. On the structure and function of different arginases. Biochim Biophys Acta. 1966 Apr 12;118(1):206–209. doi: 10.1016/s0926-6593(66)80161-3. [DOI] [PubMed] [Google Scholar]
  17. Mora J., Tarrab R., Martuscelli J., Soberón G. Characteristics of arginases from ureotelic and non-ureotelic animals. Biochem J. 1965 Sep;96(3):588–594. doi: 10.1042/bj0960588. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Porembska Z., Barańczyk A., Jachimowicz J. Arginase isoenzymes in liver and kidney of some mammals. Acta Biochim Pol. 1971;18(1):77–85. [PubMed] [Google Scholar]
  19. ROGERS S., MOORE M. Studies of the mechanism of action of the Shope rabbit papilloma virus. I. Concerning the nature of the induction of arginase in the infected cells. J Exp Med. 1963 Mar 1;117:521–542. doi: 10.1084/jem.117.3.521. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Reddy S. R., Campbell J. W. A low molecular weight arginase in the earthworm. Biochim Biophys Acta. 1968 Jul 9;159(3):557–560. doi: 10.1016/0005-2744(68)90145-9. [DOI] [PubMed] [Google Scholar]
  21. Reddy S. R., Campbell J. W. Molecular weights of arginase from different species. Comp Biochem Physiol. 1970 Feb 1;32(3):499–509. doi: 10.1016/0010-406x(70)90467-6. [DOI] [PubMed] [Google Scholar]
  22. Rossi N., Grazi E. Characterization of a new type of arginase from chicken liver. Eur J Biochem. 1969 Jan;7(3):348–352. doi: 10.1111/j.1432-1033.1969.tb19615.x. [DOI] [PubMed] [Google Scholar]
  23. SCHIMKE R. T. Adaptive characteristics of urea cycle enzymes in the rat. J Biol Chem. 1962 Feb;237:459–468. [PubMed] [Google Scholar]
  24. Shapiro A. L., Viñuela E., Maizel J. V., Jr Molecular weight estimation of polypeptide chains by electrophoresis in SDS-polyacrylamide gels. Biochem Biophys Res Commun. 1967 Sep 7;28(5):815–820. doi: 10.1016/0006-291x(67)90391-9. [DOI] [PubMed] [Google Scholar]
  25. Soberón G., Ortíz-Pineda J., Tarrab R. Characteristics of the ureotelic arginase and its role in the advent of ureotelism during the metamorphosis of the Mexican axolotl. Natl Cancer Inst Monogr. 1967 Nov;27:283–295. [PubMed] [Google Scholar]
  26. Swaney J. B., Klotz I. M. Properties of erythrocruorin from Cirraformia grandis. Arch Biochem Biophys. 1971 Dec;147(2):475–486. doi: 10.1016/0003-9861(71)90404-8. [DOI] [PubMed] [Google Scholar]
  27. Vielle-Breitburd F., Orth G. Rabbit liver L-arginase. Purification, properties, and subunit structure. J Biol Chem. 1972 Feb 25;247(4):1227–1235. [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES