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CreatorTitleDescriptionSubjectDate
1 Blumenthal, Donald K.Phosphorylation of cardiac troponin by guanosine 3':5'-monophosphate-dependent protein kinase.Homogeneous cGMP-dependent protein kinase catalyzes the rapid incorporation of phosphate, specifically into the inhibitory subunit of purified cardiac troponin with a maximal incorporation of 1 mol of phosphate/mol of troponin. When troponin was incubated in the presence of both cGMP- and cAMP-depen...Protein Kinases1978-01-25
2 Blumenthal, Donald K.Identification of the calmodulin-binding domain of skeletal muscle myosin lightIn the course of determining the primary structure of rabbit skeletal muscle myosin light chain kinase (MLCK; ATP:protein phosphotransferase, EC 2.7.1.37) a peptide fragment was obtained that appears to represent the calmodulin-binding domain of this enzyme. Low concentrations of the peptide inhibit...Peptides; Enzymes; Protein sequence1985-05
3 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; Enzymology1985-06-25
4 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 Activity1986-07-25
5 Blumenthal, Donald K.Rabbit skeletal muscle myosin light chain kinase. The calmodulin binding domain as a potential active site-directed inhibitory domain.A synthetic peptide modeled after the calmodulin (CaM)-binding domain of rabbit skeletal muscle myosin light chain kinase, Lys-Arg-Arg-Trp-Lys5-Lys-Asn-Phe-Ile-Ala10-Val-Ser-Ala-Ala-+ ++Asn15-Arg-Phe-Glycyl amide (M5), inhibited the CaM-independent chymotryptic fragment of the enzyme, C35 (Edelman, ...Synthetic Peptide1987-09-05
6 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; Metabolism1989-05-15
7 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; Enzymology1989-10-15
8 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; Peptides1995-03-31
9 Blumenthal, Donald K.; Wangsgard, Wendy P.; Meixell, Glenn E.Activation and inhibition of phosphorylase kinase by monospecific antibodies raised against peptides from the regulatory domain of the gamma-subunit.The C terminus of the catalytic gamma-subunit of phosphorylase kinase comprises a regulatory domain that contains regions important for subunit interactions and autoinhibitory functions. Monospecific antibodies raised against four synthetic peptides from this region, PhK1 (362-386), PhK5 (342-366), ...Subunit Interaction; Autoinhibitory Functions; Immunology; Antagonists & Inhibitors1995-08-30
10 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 Fragments1995-09-15
11 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 Kinase1995-09-22
12 Blumenthal, Donald K.; Underwood, Clayton J.Adaptation of the protein kinase filter paper assay to a 96-well microtiter format.The most widely used method for assaying protein kinase activities involves incorporation of radioactive phosphate into a protein or peptide substrate with subsequent binding or precipitaion of the radiolabeled substrate onto filter paper squares. We have adapted this assay for use with readily avai...Protein Kinase Activities; Filter Papers; Radioactive Phosphate1999-02-01
13 Blumenthal, Donald K.C subunits binding to the protein kinase A RI alpha dimer induce a large conformational change.We present structural data on the RI alpha isoform of the cAMP-dependent protein kinase A that reveal, for the first time, a large scale conformational change within the RI alpha homodimer upon catalytic subunit binding. This result infers that the inhibition of catalytic subunit activity is not the...Protein Kinase; cAMP2004-04-30
14 Blumenthal, Donald K.; Trewhella, JillConformationally dynamic C helix of the RIalpha subunit of protein kinase A mediates isoform-specific domain reorganization upon C subunit binding.Different isoforms of the full-length protein kinase A (PKA) regulatory subunit homodimer (R2) and the catalytic (C) subunit-bound holoenzyme (R2C2) have very different global structures despite similar molecular weights and domain organization within their primary sequences. To date, it has been th...Protein Isoforms; Global Structures; cAMP2005-10-21
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