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Phosphoprotein phosphatase activity in the thyroid.

S W Spaulding, G N Burrow

    Proceedings of the Society for Experimental Biology and Medicine. Society for Experimental Biology and Medicine (New York, N.Y.)
    |December 1, 1975
    PubMed
    Summary
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    Calf thyroid phosphoprotein phosphatase activity varies across subcellular fractions based on the substrate. Detergent treatment and DEAE chromatography further characterized these enzyme activities.

    Area of Science:

    • Biochemistry
    • Cell Biology
    • Endocrinology

    Background:

    • Phosphoprotein phosphatases are crucial enzymes involved in dephosphorylation.
    • Understanding their distribution and characteristics in specific tissues like the thyroid is important for cellular function.

    Purpose of the Study:

    • To investigate the subcellular localization of phosphoprotein phosphatase activity in calf thyroid tissue.
    • To characterize the activity of these enzymes using different substrates and detergent treatments.

    Main Methods:

    • Differential centrifugation to isolate subcellular fractions (500g, 5000g, 105,000g pellet and supernatant).
    • Assay of phosphoprotein phosphatase activity using protamine and histone as substrates.
    • Treatment with Triton X-100 to assess detergent effects on particulate fractions.

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  • DEAE ion-exchange chromatography to resolve enzyme activities in the supernatant.

    • Main Results:

    • Phosphoprotein phosphatase activity was detected in various subcellular fractions of calf thyroid.
    • Specific activity varied by fraction and substrate: protamine favored the 500g fraction, while histone favored the 5000g fraction.
    • Triton X-100 increased activity in particulate fractions, notably the 105,000g pellet.
    • DEAE chromatography revealed at least three distinct phosphoprotein phosphatase activity peaks in the 105,000g supernatant.

    Conclusions:

    • Calf thyroid phosphoprotein phosphatases exhibit distinct subcellular localizations and substrate specificities.
    • Detergent sensitivity and chromatographic behavior suggest multiple forms of these enzymes exist within thyroid cells.