Bovine cardiac muscle

The effect of phosphorylation at 13 /xmoles/g protein on functional properties was minimal. Both solubility and EAI of the phosphorylated protein were slightly higher, compared to those of intact protein (not shown). Phosphorylation with protein kinase from bovine cardiac muscle is restricted by the limited number of potential phosphorylation sites in soy proteins. Experiments are... 

Wolf, H. Hofmann, E Purification of myosin light chain kinase from bovine cardiac muscle. Proc. Natl. Acad. Sci. USA, 77, 5852-5855 (1980)... 

Herasymowych, O.S. Mani, R.S. Kay, C.M. Isolation, purification and characterization of creatine kinase from bovine cardiac muscle. Biochim. Biophys. Acta, 534, 38-47 (1978)... 

Troponin C from rabbit skeletal and bovine cardiac muscle has a molecular weight of about 18 000. Skeletal TN-C has four sites for Ca2+. Two of these (III and IV) are high affinity sites (K < 107 dm3 mol-1) which also bind Mg2+ competitively, with K = 103 dm3 mol-1. The remaining two (I and II) appear to be specific for Ca2+, although of lower affinity (K 105 dm3 mol-1).234 These two sites are the only sites in calcium-binding proteins that do not bind Mg2+ with constants in the range 102-103 dm3 mol-1. Cardiac TN-C contains two Ca2+-Mg2+ sites, one Ca2+-specific site and one low affinity site for Ca2+, in which the two aspartate residues in the skeletal TN-C protein are replaced by leucine and alanine residues.235... 

Myristoyl-CoA Protein /V-Myristoyltransferase and Myristoyl-CoA Binding Protein from Bovine Cardiac Muscle... 

Abstract Protein myristoylation refers to the cotranslational addition of a myris-toyl group to an amino-terminal glycine residue of a protein by the enzyme IV-myristoyltransferase (NMT). The myristoylation reaction depends on the availability of the cellular pools of coenzyme A and myristate and their subsequent formation of myristoyl-CoA, the substrate of NMT. In this review, we discuss NMT and myristoyl-CoA binding protein from bovine cardiac muscle which was carried out in our laboratory. 

The purpose of this review is to summarize the investigations of NMT and its binding protein from bovine cardiac muscle and its possible involvement in various signaling which have been carried out in our laboratory. 

Our laboratory has provided significant contributions in the area of myristoyla-tion. We discovered and purified the myristoyl-CoA binding protein (MCBP) from bovine cardiac muscle (Raju and Sharma 1997). In cardiac tissues there is a high level of cAMP-dependent protein kinase expression whose catalytic subunit is myristoylated (Carr et al. 1982). The catalytic subunit of cAMP-dependent protein kinase and the beta subunit of calcineurin are myristoylated proteins localized in the cytoplasm (Selvakumar et al. 2006, 2002 Rajala et al. 2000 Johnson et al. 1994 Carr et al. 1982 Aitken et al. 1982). Recently it has been shown that dephosphorylation of the catalytic subunit of myristoylated and nonmyristoylated cAMP-dependent protein kinase at Thr-197 by cellular protein phosphatase and protein... 

Raju, R. V., and Sharma, R. K. 1997. Demonstration and purification of a myristoyl-CoA binding protein from bovine cardiac muscle. Life Sci. 60 2145-2153. 

Troponin components of bovine cardiac muscle were separated by essentially the same procedure as for skeletal troponin components (Tsukui and Ebashi, 1973). Studies on the Ca + sensitivity of superprecipitation with various combinations of troponin components from rabbit skeletal and bovine cardiac muscles showed that most hybrid troponins gave the lower Ca sensitivity of superprecipitation (Ebashi, 1974a,b) (Table III). The lowest value was obtained with the combination of skeletal troponin C-T and cardiac troponin I. However, when cardiac troponin T was combined with skeletal troponin I—C, the calcium sensitivity was exceptionally high and exceeded those obtained by the native... 

Protein Kinase from Bovine Cardiac Muscle... 

The protein kinase with the most potential for food use is probably the adenosine cyclic 3, 5 -monophosphate-dependent protein kinase (cAMPdPK) from bovine cardiac muscle [76,77]. The amino acid sequence of the enzyme has been determined [78,79]. The DNA segment that encodes this kinase has been isolated, cloned, and expressed [80-82]. Thus large quantities of active enzyme could be made economically available if it proves useful in food protein modification. 

Soluble Cyclic-AMP-Dependent Protein Kinases Review of the Enzyme Isolated from Bovine Cardiac Muscle Ora Mendelsohn Rosen, Rafael Rangel-Aldao, and Jack Erlichman... 

Enzyme protein serine/threonine phosphatase (PP2A bovine cardiac muscle)... 

In addition to ChIP assays, there are open-source/web-accessible computational tools (e.g. Bailey et al., 2006) that allow researchers to find motifs in DNA or protein sequences that serve as binding sites for TF or NR. This approach could be helpful in analyzing microarray or proteomics data sets, which often uncover large numbers of seemin y co-regulated genes. Software tools can search for statistically-significant motifs within user-provided DNA sequences that may be present in some or all of the input sequences (Bailey et al, 2006). A recent study used this computational approach to search for putative TFBS in microarray data from bovine cardiac muscle (Zadissa et al, 2007). 

Rosen, O. M., Rangel-Aldao, R., and Erlichman, J., 1977, Soluble cyclic AMP-dependent protein kinases Review of the enzyme isolated from bovine cardiac muscle, in Current Topics in Cellular Regulation, Vol. 12 (B. L. Horecker and E. R. Stadtman, eds.), p. 39, Academic Press, New York. 

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