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. 1971 May;47(5):644–648. doi: 10.1104/pp.47.5.644

Purification and Properties of Amine Oxidase from Epicotyls of Pisum sativum

Roy E McGowan a,1, Robert M Muir a
PMCID: PMC396743  PMID: 16657677

Abstract

A procedure has been developed for the purification of amine oxidase (E.C. 1.4.3.4) from etiolated pea epicotyls (Pisum sativum cv. Little Marvel). The enzyme is sensitive to copper chelating reagents and carbonyl reagents, but is not inhibited by sulfhydryl reagents. The purified enzyme has a molecular weight of 1.85 × 105, as determined by sedimentation equilibrium centrifugation, and has been shown to be specifically stimulated by phosphate.

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Selected References

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  1. ANDREAE W. A. A sensitive method for the estimation of hydrogen peroxide in biological materials. Nature. 1955 May 14;175(4463):859–860. doi: 10.1038/175859a0. [DOI] [PubMed] [Google Scholar]
  2. ATKINSON D. E., HATHAWAY J. A., SMITH E. C. KINETICS OF REGULATORY ENZYMES. KINETIC ORDER OF THE YEAST DIPHOSPHOPYRIDINE NUCLEOTIDE ISOCITRATE DEHYDROGENASE REACTION AND A MODEL FOR THE REACTION. J Biol Chem. 1965 Jun;240:2682–2690. [PubMed] [Google Scholar]
  3. Achee F. M., Chervenka C. H., Smith R. A., Yasunobu K. T. Amine oxidase. XII. The association and dissociation, and number of subunits of beef plasma amine oxidase. Biochemistry. 1968 Dec;7(12):4329–4336. doi: 10.1021/bi00852a027. [DOI] [PubMed] [Google Scholar]
  4. BLASCHKO H., BUFFONI F. PYRIDOXAL PHOSPHATE AS A CONSTITUENT OF THE HISTAMINASE (BENZYLAMINE OXIDASE) OF PIG PLASMA. Proc R Soc Lond B Biol Sci. 1965 Aug 24;163:45–60. doi: 10.1098/rspb.1965.0059. [DOI] [PubMed] [Google Scholar]
  5. BUFFONI F., BLASCHKO H. BENZYLAMINE OXIDASE AND HISTAMINASE: PURIFICATION AND CRYSTALLIZATION OF AN ENZYME FROM PIG PLASMA. Proc R Soc Lond B Biol Sci. 1964 Dec 15;161:153–167. doi: 10.1098/rspb.1964.0086. [DOI] [PubMed] [Google Scholar]
  6. 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]
  7. Erwin V. G., Hellerman L. Mitochondrial monoamine oxidase. I. Purification and characterization of the bovine kidney enzyme. J Biol Chem. 1967 Sep 25;242(18):4230–4238. [PubMed] [Google Scholar]
  8. Hill J. M., Mann P. J. Further properties of the diamine oxidase of pea seedlings. Biochem J. 1964 Apr;91(1):171–182. doi: 10.1042/bj0910171. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Lantican B. P., Muir R. M. Isolation and properties of the enzyme system forming indoleacetic Acid. Plant Physiol. 1967 Aug;42(8):1158–1160. doi: 10.1104/pp.42.8.1158. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Lindell T. J., Stellwagen E. Purification and properties of phosphofructokinase from yeast. J Biol Chem. 1968 Mar 10;243(5):907–912. [PubMed] [Google Scholar]
  11. MANN P. J. Further purification and properties of the amine oxidase of pea seedlings. Biochem J. 1961 Jun;79:623–631. doi: 10.1042/bj0790623. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Panyim S., Chalkley R. High resolution acrylamide gel electrophoresis of histones. Arch Biochem Biophys. 1969 Mar;130(1):337–346. doi: 10.1016/0003-9861(69)90042-3. [DOI] [PubMed] [Google Scholar]
  13. SAYRE F. W., ROBERTS E. Preparation and some properties of a phosphateactivated glutaminase from kidneys. J Biol Chem. 1958 Nov;233(5):1128–1134. [PubMed] [Google Scholar]
  14. TABOR C. W., TABOR H., ROSENTHAL S. M. Purification of amine oxidase from beef plasma. J Biol Chem. 1954 Jun;208(2):645–661. [PubMed] [Google Scholar]
  15. YAMADA H., YASUNOBU K. T. Monoamine oxidase. I. Purification, crystallization, and properties of plasma monoamine oxidase. J Biol Chem. 1962 May;237:1511–1516. [PubMed] [Google Scholar]
  16. YAMADA H., YASUNOBU K. T. Monoamine oxidase. II. Copper, one of the prosthetic groups of plasma monoamine oxidase. J Biol Chem. 1962 Oct;237:3077–3082. [PubMed] [Google Scholar]
  17. YAMADA H., YASUNOBU K. T. The nature of the prosthetic groups of plasma amine oxidase. Biochem Biophys Res Commun. 1962 Aug 7;8:387–390. doi: 10.1016/0006-291x(62)90013-x. [DOI] [PubMed] [Google Scholar]
  18. YPHANTIS D. A. EQUILIBRIUM ULTRACENTRIFUGATION OF DILUTE SOLUTIONS. Biochemistry. 1964 Mar;3:297–317. doi: 10.1021/bi00891a003. [DOI] [PubMed] [Google Scholar]
  19. Yamasaki E. F., Swindell R., Reed D. J. Some aspects of catalysis by the amine oxidase of pea seedlings. Biochemistry. 1970 Mar 3;9(5):1206–1210. doi: 10.1021/bi00807a022. [DOI] [PubMed] [Google Scholar]

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