Calmodulin bovine brain

Harrison, J.K., Lawton, R.G., and Cnegy, M.E. (1989) Development of a novel photoreactive calmodulin derivative Cross-linking of purified adenylate cyclase from bovine brain. Biochemistry 28, 6023. 

Sharma, R. and Wang, J. H. Differential regulation of bovine brain calmodulin-dependent cyclic nucleotide phosphodiesterase isozzymesdby cyclic AMP-dependent protein kinase and calmodulin-dependent protein phosphatase. Proc. Natl Acad. Sci. U.S.A. 82 2603-2607,1986. 

Because of its ability to bind CaM, tamoxifen can increase cyclic AMP surges by inhibiting cyclic AMP hydrolysis by the Ca2+-calmodulin-dependent cyclic nucleotide phosphodiesterase (Fanidi et al. 1989 Rowlands et al. 1990). In bovine brain preparations, tamoxifen appears to act as a competitive inhibitor of calmodulin-activated phosphodiesterase with an IC50 of 2 p,M, similar to the value reported for trifluoperazine under the same experimental conditions (Lam 1984). 

Lopes MCF, Vale MGP, Carvalho AP (1990) Ca2+-dependent binding of tamoxifen to calmoduline isolated from bovine brain. Cancer Res 50 2753-2758... 

Compounds 40—43 interacted with bovine brain-calmodulin as detected in a SDS-PAGE electrophoresis. Calmodulin treated with the lactones had lower electrophoretic mobility than untreated calmodulin. The effect was comparable to that of chlorpromazine, a well known calmodulin inhibitor. In addition, different concentrations of compounds 40 and 41 inhibited calmodulin-depen dent PDEl. The inhibitory activity of herbaru-mins 1 (IC50 = 14.2 xM) and II (IC50 = 6.6 xM) was higher than that of chlorpromazine (IC50 = 9.8... 

Bartelt, D.C. Moroney, S. Wolff, D.J. Purification, characterization and substrate specificity of calmodulin-dependent myosin light-chain kinase from bovine brain. Biochem. J., 247, 747-756 (1987)... 

Additional information <1> (<1> isozyme of calmodulin-dependent multifunctional protein kinase II in smooth-muscle [5] <1> caldesmon is not a substrate of smooth-muscle myosin light-chain kinase [3] <1> no substrates are bovine cardiac C-protein, bovine brain fodrin, rabbit skeletal muscle glycogen synthase, phosphorylase B, troponon (I -I- T -I- C), actin, tropomyosin, smooth-muscle actin, filamin, vinculin, cr-actinin, protamine or phosvitin [1]) [1-3]... 

Takazawa, K. Passareiro, H. Dumont, J.E. Erneux, C. Ca /calmodulin-sensitive inositol 1,4,5-trisphosphate 3-kinase in rat and bovine brain tissues. Biochem. Biophys. Res. Commun., 153, 632-641 (1988)... 

Calmodulin from Tetrahymena presents interesting contrasts to calmodulins purified from vertebrate sources, and has, for example, 11 amino acid substitutions and one deletion of an amino acid residue compared to bovine brain calmodulin. Most of these variant residues are located near or at the III and IV Ca2+-binding sites. Tetrahymena calmodulin is very specific to... 

Figure 16.22 Structure of bovine brain calmodulin. See Chapter 4 for amino acid abbreviations. (Reproduced by permission from Klee CB, Crouch TH, Richman PG. Calmodulin. Annu Rev Biochem 49 489-515, 1980.)...

Because of the known requirement of calmodulin for the catalytic activity of NOS, the possibility of alteration in the interaction of calmodulin with NOS during preincubation was tested. The exogenous addition of bovine brain calmodulin during the preincubation did not reverse NOS... 

Calmodulin from spinach leaves (CaM ) or bovine brain (CaM ). 

Cox and Harrison (1983) have reported observations giving the relative inhibition of calmodulin activity, in vitro, caused by 13 divalent metal ions. The metal-ion concentration required to produce a 50% reduced activation of cyclic nucleotide phosphodiesterase with bovine brain calmodulin (1050) was chosen as a measure of calmodulin inhibition in vitro. On the basis of the 1050 values, the ranking for the effectiveness of the 13 divalent metal ions studied was Hg2 > Cu " > Pt > Cd = Be " > Zn2+ > Pb > Ba = Pd > Co > Ni " > Mn2" > Sr2. ... 

In contrast, bovine brain calmodulin interacts with phosphodiesterase in a way that does not reveal any heterogeneity in binding sites. 

Figure 4, Separation of calmodulin from bovine brain extract using a weak anion-exchanger. Column., 4.6 mm X 50 mm, 5 micron BAKERBOND WP-PEI mobile phase, initial buffer (A) 25 mM Tris, pH 7.0 final buffer (B) 2.0 M sodium acetate, pH 5.0 gradient, 0—100% B in 15 min flow-rate, 1 ml/min d ectkn UV f280 nml sample. 1.0 ml fl.O g bovine brain extract dissolved in 100 ml of buffer Aand centrifuged. Protein concentration —8 mg/ml.) Peaks CaM, calmodulin.

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