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Mode of inactivation of putrescine oxidase by 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide or metal ions.

Mode of inactivation of putrescine oxidase by 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide or metal ions. Research Abstract Details 

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  • Mode of inactivation of putrescine oxidase by 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide or metal ions. Abstract Text:

    m okadaM Okada,s kawashimaS Kawashima,k imahoriK Imahori,

    1. Putrescine oxidase [EC 1.4.3.10] was partially inactivated by reaction with 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide (EDC), rapidly. The activity of the modified enzyme toward putrescine was 5.6% of that of the native enzyme. Moreover, the optimal pH and Km value of the modified enzyme for putrescine changed from 9.0 to 10.5 and from 0.23 to 3.4 mM, respectively. This modified enzyme showed activity toward monoamines such as n-butylamine, n-hexylamine, and n-octylamine, which are not substrates of the native enzyme. 2. Heavy metal ions inactivated putrescine oxidase completely. Hg2+ had the stronger ability to inactivate it. This inactivation was due to the dissociation of FAD from the enzyme molecule. The Fad-free enzyme had no ability to reassociate FAD, in contrast to the apoenzyme. The enzyme treated with Hg2+ showed characteristic behavior on SDS-polyacrylamide gel electrophoresis. 3. From the results of chemical modification it was deduced that a carboxyl group plays an important role in binding the substrate.

    Mode of inactivation of putrescine oxidase by 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide or metal ions. Publishing Authors By Initials

    m okadaM Okada,s kawashimaS Kawashima,k imahoriK Imahori,

    For similar biochemical phenomena, metabolism, and nutrition: biochemical phenomena: substrate specificity research abstracts see: biochemical phenomena, metabolism, and nutrition: biochemical phenomena: substrate specificity research

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    Mode of inactivation of putrescine oxidase by 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide or metal ions. Journal Published:

    PUBLICATION TYPE: Journal Article

    Journal: Journal of biochemistry

    VOLUME: 88

    Page Numbers: 481-8

    Journal Abbreviation: J. Biochem.

    ISSN: 0021-924X

    DAY: 19

    MONTH: Aug

    YEAR: 1980

    Mode of inactivation of putrescine oxidase by 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide or metal ions. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 376600

    Mode of inactivation of putrescine oxidase by 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide or metal ions. Keywords Mesh Terms:

    KEYWORDS: Substrate Specificity

    MESH TERMS: antagonists & inhibitors

    Chemical & Substance for Abstract: Mode of inactivation of putrescine oxidase by 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide or metal ions. Information

    Substance Name: Oxidoreductases Acting on CH-NH Group Do

    Registry Number: EC 1.5.-

    Grant and Affiliation Information for Mode of inactivation of putrescine oxidase by 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide or metal ions.

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    Country: JAPAN

    JAPAN Research PublicationJAPAN Research Publication

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    MEDLINETA: J Biochem

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    Mode of inactivation of putrescine oxidase by 1-ethyl-3-3-dimethylaminopropylcarbodiimide or metal ions Related Publications

     

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