What question did this study set out to answer?

The aim is to explore the substrate specificity and inhibition mechanisms of phospholipid-sensitive Ca2+-dependent protein kinase from bovine heart.

Phospholipid-sensitive Ca2+-dependent protein kinase from heart. II. Substrate specificity and inhibition by various agents.

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Population

Phospholipid-sensitive Ca2+-dependent protein kinase purified from bovine heart, rat brain, and pig spleen

Design

Preclinical

Authors

Identifies optimal PKC substrates in bovine heart; extends biochemical profiling but leaves human cardiac relevance open.

The aim is to explore the substrate specificity and inhibition mechanisms of phospholipid-sensitive Ca2+-dependent protein kinase from bovine heart.
Purified the enzyme to 80-95% homogeneity from bovine heart.
Evaluated the apparent Km for ATP and identified inhibition by various agents.
Examined substrate usage with histone H1 and myelin basic protein.
Apparent Km for ATP using histone H1 was 4.4 μM.
Histone H1 and myelin basic protein were the best substrates with Km values of 0.6 μM and 0.3 μM, respectively.
Inhibition was strongest with alpha,beta-methylene ATP.

Population

Phospholipid-sensitive Ca2+-dependent protein kinase purified from bovine heart, rat brain, and pig spleen

Intervention

Various substrates (including histone H1 and myelin basic protein) and inhibitors

Outcome

Substrate specificity (Km, Vmax) and enzyme inhibitionsurrogate

The study characterizes the substrate specificity and inhibition profile of phospholipid-sensitive Ca2+-dependent protein kinase from the heart.

Wise et al. (1982) studied this question.

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