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The inhibition and activation of polyamine oxidase from oat seedlings

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Polyamines in Plants

Part of the book series: Advances in Agricultural Biotechnology ((AABI,volume 18))

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Abstract

In a homologous series of di-guanidines (NH2C(= NH)NH(CH2)xNHC(=KH) NH2,) where x = 2–12, greatest inhibition of polyamine oxidase was found with x = 8.The synthetic fungicide guazatine

was particularly effective as an inhibitor of polyamine oxidase, with Ki of ca 10− 8 M. Inhibition due to the triamine derived from guazatine by hydrolysis was less effective by a factor of ca 200. Comparison of various inorganic salts at 1 M showed that polyamine oxidase activity was enhanced in the order RbCl > KCl > KBr > NH4Cl > NaNO3 > LiCl = NaCl > control (no salt) > CaCl2 = MgCl2. Activity in RbCl was about 4 to 5 times greater than in the salt-free control. Enzyme activity is rapidly lost during assay. This loss of activity could not be attributed to inhibition by aminopropylpyrroline effect on enzyme activity.

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© 1985 Martinus Nijhoff/Dr W. Junk Publishers, Dordrecht

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Smith, T.A. (1985). The inhibition and activation of polyamine oxidase from oat seedlings. In: Galston, A.W., Smith, T.A. (eds) Polyamines in Plants. Advances in Agricultural Biotechnology, vol 18. Springer, Dordrecht. https://doi.org/10.1007/978-94-009-5171-6_6

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  • DOI: https://doi.org/10.1007/978-94-009-5171-6_6

  • Publisher Name: Springer, Dordrecht

  • Print ISBN: 978-94-010-8788-9

  • Online ISBN: 978-94-009-5171-6

  • eBook Packages: Springer Book Archive

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