Inhibition of alanine aminotransferase activity by IgG.

DOI Web Site 1 Citations 14 References
  • Ando Toshiko
    Department of Clinical Laboratories, Yokohama City University Hospital
  • Watanabe Shinichiro
    Department of Clinical Laboratories, Yokohama City University Hospital
  • Okawa Kiyo
    Department of Clinical Laboratories, Yokohama City University Hospital
  • Ogawa Noboru
    Department of Clinical Laboratories, Yokohama City University Hospital
  • Ehara Shigeru
    Department of Clinical Laboratories, Yokohama City University Hospital
  • Nagasawa Yoshimi
    健康保険組合連合会大阪中央病院中央検査部
  • Ishihara Jyun
    静岡県立こども病院臨床病理科
  • Kameko Fumiko
    信州大学医学部保健学科検査技術科学専攻
  • Fujita Kiyotaka
    信州大学医学部保健学科検査技術科学専攻

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Other Title
  • ＡＬＴ活性阻害を示すＩｇＧの免疫化学的特性
  • ALT カッセイ ソガイ オ シメス IgG ノ メンエキ カガクテキ トクセイ

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Abstract

We observed a 74-year old woman with chronic hepatitis C, whose alanine aminotransferase (L-Alanine: 2-oxoglutarate aminotransferase: EC.2.6. 1.2; ALT) activity in serum was below 2 IU/L (reference value: 9-25 IU/L). ALT activity in normal human serum was inhibited when the patient's serum was added to normal serum. By immunoprecipitation assay, it was found that the patient's IgG-κ acted as an inhibitor of ALT. The ALT inhibition of the patient's IgG was not blocked by adding alanine as a substrate, and also by adding pyridoxal phosphate as a coenzyme. The purified patient's IgG was found to be composed of two γ chains of about 50kDa and two κ chains of 28kDa by SDS-PAGE. The inhibitory ability of IgG was exclusively located in the Fab region of the molecule.

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