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Developmental changes in rat hepatic casein kinases 1 and 2.
1Departament de Bioquímica i Biologia Molecular, Facultat de Ciències, Universitat Autònoma de Barcelona, Spain.
European Journal of Biochemistry
|December 30, 1987
Summary
Cytosolic histone and casein kinase activities peak during late fetal development and decline after birth. Insulin administration alters the affinity of these enzymes in developing rat liver.
Area of Science:
- Biochemistry
- Developmental Biology
- Molecular Endocrinology
Background:
- Cytosolic histone and casein kinases are crucial enzymes involved in cellular regulation.
- Understanding their activity during liver development is essential for comprehending developmental processes.
Purpose of the Study:
- To investigate the developmental changes in cytosolic histone and casein kinase activities and their kinetic properties in rat liver.
- To examine the effect of insulin on these enzymes during the postnatal period.
Main Methods:
- Enzyme activity assays were performed on cytosolic extracts from rat livers at various fetal and postnatal stages.
- Kinetic parameters, including Km values for casein and ATP, were determined.
- The impact of insulin administration on enzyme kinetics was assessed.
Main Results:
- Both histone and casein kinase activities exhibited a peak at day 21 of gestation, decreasing significantly by birth.
- Casein kinase 1 and casein kinase 2 activities showed developmental variations, as did their affinity for casein (Km values).
- Insulin administration to one-day-old rats altered the Km values of both casein kinase 1 and 2.
Conclusions:
- Cytosolic histone and casein kinase activities and their substrate affinities undergo significant modulation during rat liver development.
- Insulin plays a role in regulating the kinetic properties of these kinases postnatally.