Filters: Department: "Biomedical Informatics" School Or College: "College of Pharmacy" Collection: "ir_uspace"
1 - 25 of 4
| Creator | Title | Description | Subject | Date | ||
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Blumenthal, Donald K. | Characterization of the phosphotyrosyl protein phosphatase activity of calmodulin-dependent protein phosphatase. | Calmodulin-dependent protein phosphatase from bovine brain and heart was assayed for phosphotyrosine and phosphoserine phosphatase activity using several substrates: 1) smooth muscle myosin light chain (LC20) phosphorylated on tyrosine or serine residues, 2) angiotensin I phosphorylated on tyrosine,... | Metabolism; Phosphatase Activity | 1986-07-25 |
| 2 |
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Blumenthal, Donald K. | Effects of deletions in the central helix of calmodulin on enzyme activation and peptide binding. | Using site-directed mutagenesis we have expressed in Escherichia coli three engineered calmodulins (CaM) containing deletions in the solvent-exposed region of the central helix. These are CaM delta 84, Glu-84 removed; CaM delta 83-84, Glu-83 and Glu-84 removed; and CaM delta 81-84, Ser-81 through Gl... | Drug Effects; Genetics; Metabolism | 1989-05-15 |
| 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 |
| 4 |
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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 |
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