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Related Experiment Videos

Isolation and characterization of monoamine oxidase from hyperfunctioning human thyroid

A Udupa, S Srinivasan, K N Udupa

    Indian Journal of Physiology and Pharmacology
    |July 1, 1976
    PubMed
    Summary

    Human thyroid monoamine oxidase (MAO) was isolated from hyperfunctioning thyroids. The active enzyme component with a molecular weight of 4000 was identified, suggesting MAO may exist in multiple forms.

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    Area of Science:

    • Biochemistry
    • Enzymology
    • Thyroid Research

    Background:

    • Investigating the biochemical properties of human thyroid monoamine oxidase (MAO) in hyperfunctioning conditions.
    • Understanding the potential for multiple forms of MAO in thyroid tissue.

    Observation:

    • Human thyroid mitochondria were isolated and purified.
    • Monoamine oxidase (MAO) was purified using DEAE-column and Sephadex G-200 chromatography.
    • Three molecular weight components (220,000, 23,000, and 4000) were detected, with the 4000 MW component exhibiting enzyme activity.

    Findings:

    • The active form of human thyroid monoamine oxidase (MAO) has a molecular weight of approximately 4000.
    • Analysis of patient blood revealed plasma MAO, RBC cholinesterase, plasma histaminase, and plasma catecholamines.

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  • Histological and histochemical examinations of thyroid tissues were performed.

    • Implications:

    • The findings support the hypothesis that monoamine oxidase (MAO) may exist in multiple molecular forms within the human thyroid.
    • This research contributes to understanding thyroid pathophysiology and enzyme kinetics.
    • Further investigation into the distinct roles of different MAO forms could reveal new therapeutic targets.