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| Creator | Title | Description | Subject | Date | ||
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Blumenthal, Donald K. | Characterization of the calmodulin-binding and catalytic domains in skeletal muscle myosin light chain kinase. | Limited proteolysis has been utilized to study the structural organization of rabbit skeletal muscle myosin light chain kinase. The enzyme (Mr approximately 89,000 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis) consists of an amino-terminal, protease-susceptible region of unidentified... | Enzymology; Skeletal Muscle; Proteolysis, Peptide Fragments | 1995-09-15 |
| 2 |
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Blumenthal, Donald K. | Dephosphorylation of cAMP-dependent protein kinase regulatory subunit (type II) by calmodulin-dependent protein phosphatase. Determinants of substrate specificity. | Calmodulin-dependent protein phosphatase purified from bovine cardiac muscle catalyzed the rapid dephosphorylation of Ser-95 of bovine cardiac cAMP-dependent protein kinase regulatory subunit (RII). The kinetic constants determined for the reaction (Km = 20 microM; Vmax = 2 mumol min-1 mg-1) are com... | Metabolism; High Pressure Liquid; Enzymology | 1985-06-25 |
| 3 |
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Blumenthal, Donald K. | Gamma-subunit of skeletal muscle phosphorylase kinase contains two noncontiguous domains that act in concert to bind calmodulin. | Phosphorylase kinase is a Ca2+-regulated, multisubunit enzyme that contains calmodulin as an integral subunit (termed the delta-subunit). Ca2+-dependent activity of the enzyme is thought to be regulated by direct interaction of the delta-subunit with the catalytic subunit (the gamma-subunit) in the ... | Pharmacology; Metabolism; Enzymology | 1989-10-15 |
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