Clinical significance of serum monoamine oxidase activities determined by ammonia method using n-butylamine as substrates

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  • ITO Susumu
    Second Department of the Internal Medicine, School of Medicine, Tokushima University
  • TAKAOKA Takashi
    Second Department of the Internal Medicine, School of Medicine, Tokushima University
  • KISHI Seiichiro
    Second Department of the Internal Medicine, School of Medicine, Tokushima University
  • FUJII Setsuro
    Department of Enzyme Physiology Institute for Enzyme Research, School of Medicine, Tokushima University (Tokushima)
  • OKUDA Hiromichi
    Department of Enzyme Physiology Institute for Enzyme Research, School of Medicine, Tokushima University (Tokushima)

Bibliographic Information

Other Title
  • Ammonia直接比色定量法を応用したMonoamine oxidase測定法の臨床的意義について
  • Ammonia チョクセツ ヒショク テイリョウホウ オ オウヨウ シタ Monoamine oxidase ソクテイホウ ノ リンショウテキ イギ ニ ツイテ

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Description

New methods for the determinations of monoamine oxidase (MAO) activities were presented using benzylamine (BZA-oxidase) or n-butylamine (NBA-oxidase) as substrates, in which the amounts of ammonia liberated by the enzyme actions were measured by means of the direct colorimetric method of Okuda and Fujii. BZA-oxidase was higher than NBA-oxidase in liver extract, but the relation was reversed in serum. It was felt that MAO found in liver and in serum might not be the same. Serum MAO activities increased more markedly in liver cirrhosis and hepatic cancer than in acute or chronic hepatitis. It was interesting enough that the increased serum MAO activities were closely related with the grades of fibrosis determined histologically. It was considered that the n-butylamine was the preferable substrates than the benzylamine for the determination of serum MAO activities, because NBA-oxidase activities were higher than those of BZA-oxidase in human serum.

Journal

  • Kanzo

    Kanzo 15 (5), 301-309, 1974

    The Japan Society of Hepatology

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