Jan 20, 1976

Glial fibrillary acidic protein from bovine and rat brain. Degradation in tissues and homogenates

Biochimica Et Biophysica Acta
D Dahl


Compared with human material glial fibrillary acidic protein isolated from bovine, rat and mouse brain was remarkably homogeneous and migrated as a single band at 54 000 mol. wt. on sodium dodecyl sulfate gel electrophoresis. The protein was extremely susceptible to proteolysis and lower molecular weight components were invariably isolated together with the major species when the brain was not rapidly frozen. Further degradation of the 54 000 mol wt. polypeptide in bovine tissues incubated at 24 degrees C resulted in preparations essentially identical to those previously isolated from human autopsy material and separating into a series of immunologically active polypeptides ranging in molecular weight from 54 000 to approximately 40 500. The gel band pattern obtained after progressively longer periods of autolysis suggested that small fragments were cleaved from the original polypeptide in successive steps of degradation. As in human brain, the lower molecular weight products in the 45 000-40 500 range were more resistant to proteolysis and still present after prolonged periods of tissue autolysis. The effect of the pH and of proteinase inhibitors on degradation was studied in homogenates of bovine brain stem incubated at 37 de...Continue Reading

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Mentioned in this Paper

Macromolecular Compounds
Glial Fibrillary Acidic Protein
Proteinase inhibitors, antifibrinolytic
Bos taurus
Malignant Neoplasm of Brain Stem
Cytokinesis of the Fertilized Ovum

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