Abstract
Guanosine 3′: 5′-momophosphate-dependent protein kinase from bovine heart muscle was purified to apparent homogeneity using affinity chromatography. The kinase activity was purified at least 16.400-fold with an overall recovery of 6%. Sodium dodecyl sulfate gels of purified kinase showed one stained band corresponding to a molecular weight of 82.000. When histone I was used as substrate protein, half maximal stimulation of kinase activity by cGMP and cAMP was observed at concentrations of 0.025 and 6.8 M, respectively. Low concentrations of magnesium acetate(2mM) were necessary for phosphorylation of histone I. In contrast, optimal phosphorylations rates in the presence of histone IIb (0.2 mg/ml) were obtained in the presence of 60 mM magnesium acetate. It is suggested, that high concentrations of magnesium are required only for the phosphorylation of histone IIb.
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© 1978 Springer-Verlag Berlin Heidelberg
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Flockerzi, V., Speichermann, N., Hofmann, F. (1978). Purification And Characterisation Of A cGMP-Dependent Protein Kinase From Bovine Heart Muscle. In: Deutsche Pharmakologische Gesellschaft. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-662-39532-5_99
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DOI: https://doi.org/10.1007/978-3-662-39532-5_99
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-662-38666-8
Online ISBN: 978-3-662-39532-5
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