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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. | Characterization of the regulatory domain of the gamma-subunit of phosphorylase kinase. The two noncontiguous calmodulin-binding subdomains are also autoinhibitory. | Phosphorylase kinase is a multimeric protein kinase (alpha 4 beta 4 gamma 4 delta 4) whose enzymatic activity is conferred by its gamma-subunit. A library of 18 overlapping synthetic peptides spanning residues 277-386 of the gamma-subunit has been prepared to use in identifying important regulatory ... | Metabolism; Phosphorylase Kinase | 1995-09-22 |
| 3 |
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Blumenthal, Donald K. | Identification of the substrate and pseudosubstrate binding sites of phosphorylase kinase gamma-subunit. | Using site-directed mutagenesis, we proposed that an autoinhibitory domain(s) is located at the C-terminal region (301-386) of the phosphorylase kinase gamma-subunit (Huang, C.-Y.F., Yuan C.-J., Livanova, N.B., and Graves, D.J. (1993) Mol. Cell. Biochem. 127/128, 7-18). Removal of the putative inhib... | Mutagenesis; Autoinhibitory Domain; Peptides | 1995-03-31 |
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