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Related Experiment Videos

Liver glycogen synthase in the developing foetal rat.

C Watts, K R Gain

    Biochimica Et Biophysica Acta
    |May 14, 1981
    PubMed
    Summary

    Liver glycogen synthase activity increases significantly in late gestation and after birth. Fetal liver shows a reduced affinity for UDPglucose compared to adult liver, requiring careful interpretation of synthesis rates.

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    Area of Science:

    • Biochemistry
    • Developmental Biology
    • Enzymology

    Background:

    • Liver glycogen synthase (LGS) is crucial for glycogen synthesis.
    • Understanding LGS kinetics during fetal development is essential for assessing metabolic maturation.

    Purpose of the Study:

    • To determine kinetic constants of liver glycogen synthase in fetal liver during late gestation and early postnatal life.
    • To compare fetal LGS kinetic parameters with those of adult liver.

    Main Methods:

    • Assay of liver glycogen synthase activity and kinetic constants (Vmax, Km) in fetal and newborn liver homogenates.
    • Removal of amylase-like contaminants from fetal samples prior to radioassay.

    Main Results:

    • Vmax of both inactive and active LGS increased markedly from late gestation to birth.
    • Km for UDPglucose of active LGS was significantly higher in fetal liver compared to adult liver.
    • Km values for active LGS decreased from day 19 of gestation to the newborn period.

    Conclusions:

    • Fetal liver exhibits a reduced affinity for UDPglucose, impacting in vivo glycogen synthesis rate estimations.
    • Assays of fetal liver enzymes require careful methodology, including contaminant removal and consideration of developmental differences.
    • Kinetic properties of LGS mature significantly during late gestation and early postnatal development.

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