November 1, 1987Biochemical JournalOpen Access

Purification, characterization and substrate specificity of calmodulin-dependent myosin light-chain kinase from bovine brain

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Population

Bovine brain tissue and various protein substrates including turkey gizzard myosin light chain and rabbit…

Design

Preclinical

Authors

DBDiana C. BarteltUniversity of North Carolina at Chapel Hill SMSimon E. MoroneyMorphoSys (Germany)DWDonald J. WolffRutgers, The State University of New Jersey

Discussion

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Implication

No immediate clinical implications; leaves open MLCK isoform studies in human cardiovascular tissues.

Structured PICO

Population

Bovine brain tissue (source of MLCK) and various protein substrates including turkey gizzard myosin light chain and rabbit skeletal-muscle myosin light chain

Intervention

Purification and biochemical characterization of calmodulin-dependent myosin light-chain kinase (MLCK)

Outcome

Substrate specificity, specific activity, and phosphorylation characteristics of purified MLCKsurrogate

Bovine brain MLCK is a 152,000 Da protein that specifically phosphorylates myosin light chains and is regulated by calmodulin and cyclic-AMP-dependent protein kinase.

Cite This Study

Bartelt et al. (1987) studied this question.

synapsesocial.com/papers/6a208eecb15f64b498301f4c https://doi.org/10.1042/bj2470747

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Purification, characterization and substrate specificity of calmodulin-dependent myosin light-chain kinase from bovine brain

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Purification, characterization and substrate specificity of calmodulin-dependent myosin light-chain kinase from bovine brain

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Also Consider

Also Consider