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. 1974 Jul;142(1):27–35. doi: 10.1042/bj1420027

The distribution of l-asparagine synthetase in the principal organs of several mammalian and avian species

Harry A Milman 1, David A Cooney 1
PMCID: PMC1168207  PMID: 4216348

Abstract

A survey was conducted of the distribution of l-asparagine synthetase and of l-asparaginase in the principal organs of representative mammals and birds. Although a radiometric assay was used as a routine, several additional criteria, including enzymic and chromatographic ones, were used to verify that the product of the synthetase was l-asparagine. Recoveries of exogenous l-asparagine were assessed in the presence of a number of mouse organs and found to be about 85%. In addition, evidence is presented for the existence in mouse liver of a thermolabile activity capable of destroying l-asparagine and stimulated by high concentrations of NH4+ ions. Of the organs surveyed, pancreas was generally found to synthesize l-asparagine at the most rapid rate, whereas extracts of liver catalysed the decomposition of this amide at the greatest velocity. Of the species studied, guinea pig had the highest activities of pancreatic l-asparagine synthetase and also of hepatic l-asparaginase. The pancreas of mouse and ox also were good sources of l-asparagine synthetase.

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Selected References

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

  1. Benuck M., Stern F., Lajtha A. Formation of asparagine from aspartic acid in rat brain. J Neurochem. 1970 Aug;17(8):1133–1141. doi: 10.1111/j.1471-4159.1970.tb03361.x. [DOI] [PubMed] [Google Scholar]
  2. Bonetti E., Abbondanza A., Della Corte E., Stirpe F. The regulation of L-asparaginase activity in rats and mice. Effects of normal and malignant growth, of sex and of dietary changes. Biochem J. 1969 Nov;115(3):597–601. doi: 10.1042/bj1150597. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Cassano G. B., Hansson E. Uptake of [14C]glutamine in the tissues of the mouse studied by whole-body autoradiography. J Neurochem. 1965 Sep-Oct;12(9):851–855. doi: 10.1111/j.1471-4159.1965.tb10270.x. [DOI] [PubMed] [Google Scholar]
  4. Cooney D. A., Capizzi R. L., Handschumacher R. E. Evaluation of L-asparagine metabolism in animals and man. Cancer Res. 1970 Apr;30(4):929–935. [PubMed] [Google Scholar]
  5. Cooney D. A., Milman H. A., Truitt R. Disposable and versatile vessels for microdiffusion studies. Anal Biochem. 1971 Jun;41(2):583–589. doi: 10.1016/0003-2697(71)90182-5. [DOI] [PubMed] [Google Scholar]
  6. Holcenberg J. S. Guinea pig asparagine synthetase. Biochim Biophys Acta. 1969 Jul 8;185(1):228–238. doi: 10.1016/0005-2744(69)90297-6. [DOI] [PubMed] [Google Scholar]
  7. Horowitz B., Madras B. K., Meister A., Old L. J., Boyes E. A., Stockert E. Asparagine synthetase activity of mouse leukemias. Science. 1968 May 3;160(3827):533–535. doi: 10.1126/science.160.3827.533. [DOI] [PubMed] [Google Scholar]
  8. Horowitz B., Meister A. Glutamine-dependent asparagine synthetase from leukemia cells. Chloride dependence, mechanism of action, and inhibition. J Biol Chem. 1972 Oct 25;247(20):6708–6719. [PubMed] [Google Scholar]
  9. 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]
  10. Ohnuma T., Bergel F., Bray R. C. Enzymes in cancer. Asparaginase from chicken liver. Biochem J. 1967 Apr;103(1):238–245. doi: 10.1042/bj1030238. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Patterson M. K., Jr, Orr G. R. Regeneration, tumor, dietary, and L-asparaginase effects on asparagine biosynthesis in rat liver. Cancer Res. 1969 Jun;29(6):1179–1183. [PubMed] [Google Scholar]
  12. RAVEL J. M., NORTON S. J., HUMPHREYS J. S., SHIVE W. Asparagine biosynthesis in Lactobacillus arabinosus and its control by asparagine through enzyme inhibition and repression. J Biol Chem. 1962 Sep;237:2845–2849. [PubMed] [Google Scholar]
  13. Ressler C., Nagarajan G. R., Lauinger C. Biosynthesis of asparagine from beta-L-[4C-15N]cyanoalanine in Lathyrus sylvestris W. seedlings. Origin of the amide nitrogen. Biochim Biophys Acta. 1969 Sep 2;184(3):578–582. doi: 10.1016/0304-4165(69)90271-2. [DOI] [PubMed] [Google Scholar]
  14. TURSKY T., VALOVICOVA E. ASPARAGINASE IN THE BRAIN OF GUINEA PIG IN EXPERIMENTAL ALLERGIC ENCEPHALOMYELITIS. J Neurochem. 1964 Feb;11:99–108. doi: 10.1111/j.1471-4159.1964.tb06746.x. [DOI] [PubMed] [Google Scholar]
  15. Tate S. S., Meister A. Studies on the sulfhydryl groups of L-aspartate beta-decarboxylase. Biochemistry. 1968 Sep;7(9):3240–3247. doi: 10.1021/bi00849a029. [DOI] [PubMed] [Google Scholar]
  16. Woods J. S., Handschumacher R. E. Hepatic homeostasis of plasma L-asparagine. Am J Physiol. 1971 Dec;221(6):1785–1790. doi: 10.1152/ajplegacy.1971.221.6.1785. [DOI] [PubMed] [Google Scholar]

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