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. 1971 Feb;41(2):294–301. doi: 10.1111/j.1476-5381.1971.tb08030.x

Decarboxylases of histidine and ornithine in chick embryo

Yao C G Dz[unk]dz[unk]e, Elsa Rosengren
PMCID: PMC1703295  PMID: 5572279

Abstract

1. The activities of histidine and ornithine decarboxylases as well as the histamine content of the developing chick embryo were studied.

2. Histidine decarboxylase (L-histidine carboxy-lyase; E.C. 4.1.1.22) activity was fairly low with a tendency to increase at later stages of development. This enzyme was preferentially present in the supernatant fraction of the tissue homogenate. α-Methyl-histidine, but not α-methyl-DOPA, inhibited its activity.

3. The histamine content per gramme of embryo was low with a tendency to increase with the age of the embryo.

4. Ornithine decarboxylase (L-ornithine carboxy-lyase; E.C. 4.1.1.17) activity was high at the beginning of the stages of development investigated, but later there was a steep fall in activity. A noticeable feature was that while the activity in the residual fraction of the homogenate remained almost constant during development, the activity in the supernatant fraction was high in the early stages, then fell rapidly to nearly zero at later stages.

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Selected References

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

  1. Caldarera C. M., Barbiroli B., Moruzzi G. Polyamines and nucleic acids during development of the chick embryo. Biochem J. 1965 Oct;97(1):84–88. doi: 10.1042/bj0970084. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Code C. F. The quantitative estimation of histamine in the blood. J Physiol. 1937 Apr 9;89(3):257–268. doi: 10.1113/jphysiol.1937.sp003476. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Grahn B., Hughes R., Kahlson G., Rosengren E. Retardation of protein synthesis in rat foetal liver on inhibiting rate of histamine formation. J Physiol. 1969 Feb;200(3):677–685. doi: 10.1113/jphysiol.1969.sp008716. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Grahn B., Rosengren E. Adrenaline induced acceleration of histamine formation in vitro, studied by two isotopic methods. Br J Pharmacol Chemother. 1968 Jul;33(3):472–479. doi: 10.1111/j.1476-5381.1968.tb00495.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Grahn B., Rosengren E. Retardation of protein synthesis in rat tumours on inhibiting histamine formation. Experientia. 1970;26(2):125–126. doi: 10.1007/BF01895530. [DOI] [PubMed] [Google Scholar]
  6. KAHLSON G., ROSENGREN E., THUNBERG R. OBSERVATIONS ON THE INHIBITION OF HISTAMINE FORMATION. J Physiol. 1963 Dec;169:467–486. doi: 10.1113/jphysiol.1963.sp007273. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. KOBAYASHI Y. Determination of histidine decarboxylase activity by liquid scintillation counting of C-14-O2. Anal Biochem. 1963 Apr;5:284–290. doi: 10.1016/0003-2697(63)90080-0. [DOI] [PubMed] [Google Scholar]
  8. Kahlson G., Rosengren E. New approaches to the physiology of histamine. Physiol Rev. 1968 Jan;48(1):155–196. doi: 10.1152/physrev.1968.48.1.155. [DOI] [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. Levine R. J., Watts D. E. A sensitive and specific assay for histidine decarboxylase activity. Biochem Pharmacol. 1966 Jul;15(7):841–849. doi: 10.1016/0006-2952(66)90161-4. [DOI] [PubMed] [Google Scholar]
  11. MOYED H. S., MAGASANIK B. The biosynthesis of the imidazole ring of histidine. J Biol Chem. 1960 Jan;235:149–153. [PubMed] [Google Scholar]
  12. Pegg A. E., Williams-Ashman H. G. Biosynthesis of putrescine in the prostate gland of the rat. Biochem J. 1968 Jul;108(4):533–539. doi: 10.1042/bj1080533. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Russell D., Snyder S. H. Amine synthesis in rapidly growing tissues: ornithine decarboxylase activity in regenerating rat liver, chick embryo, and various tumors. Proc Natl Acad Sci U S A. 1968 Aug;60(4):1420–1427. doi: 10.1073/pnas.60.4.1420. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. SCHAYER R. W. Formation and binding of histamine by rat tissues in vitro. Am J Physiol. 1956 Sep;187(1):63–65. doi: 10.1152/ajplegacy.1956.187.1.63. [DOI] [PubMed] [Google Scholar]
  15. SHEDLOVSKY A. E., MAGASANIK B. A defect in histidine biosynthesis causing an adenine deficiency. J Biol Chem. 1962 Dec;237:3725–3730. [PubMed] [Google Scholar]
  16. SHEDLOVSKY A. E., MAGASANIK B. The enzymatic basis of an adenine-histidine relationship in Escherichia coli. J Biol Chem. 1962 Dec;237:3731–3736. [PubMed] [Google Scholar]
  17. SPRINSON D. B., RITTENBERG D. The metabolic reactions of carbon atom 2 of L-histidine. J Biol Chem. 1952 Oct;198(2):655–661. [PubMed] [Google Scholar]

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