Myosin, rabbit skeletal

Figure 11.9 (Left) The EF hand helix-loop-helix motif (centre) rat testes calmodulin. The globular domains each have two Ca2+-binding sites, indicated by white spheres, connected by a seven-turn a-helix (right) two views of the (Ca2+)4 fruit fly calmodulin in complex with its 26-residue target peptide from rabbit skeletal muscle myosin light chain kinase, ((left, centre) From Voet and Voet, 2004. Reproduced with permission from John Wiley Sons., Inc. and (right) Carafoli, 2002. Copyright (2002) National Academy of Sciences, USA.)...

Nagamoto, H. Yagi, K. Properties of myosin light chain kinase prepared from rabbit skeletal muscle by an improved method. J. Biochem., 95, 1119-1130 (1984)... 

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]... 

Boyer, C., Joandel, S., Ouali, A., and Celioli, J. 1996. Determination of surface hydrophobicity of fast and slow myosins from rabbit skeletal muscles Implication in heat-induced gelation. J. Sci. Food Agric. 72 367-375. 

J Frank, G., and Weeds, A. G. The amino-acid sequence of the alkali light chains of rabbit skeletal-muscle myosin. Eur. J. Biochem. 44, 317-334 (1974). 

Parry, D. A. D. (1981). Structure of rabbit skeletal myosin Analysis of the amino acid sequences of two fragments from the rod region./. Mol. Biol. 153, 459-464. 

There is a great deal of literature on the kinetics of myosin SI (crossbridge) ATPase. Originally biochemical studies were restricted to rabbit skeletal myosin. However, recent studies have often been conducted on... 

Studies of the pyrene label on actin indicate that the ATP-induced dissociation of actin occurs via a three-step process (steps 1, 2, and c, Scheme 1 Millar and Geeves, 1983). Initial fast equilibrium binding of ATP (controlled by and probably diffusion limited) is followed by an isomerization that alters the environment of the pyrene label on actin. This isomerization is fast in myosin II and much slower for some non-muscle myosins (-500 s-1 for Dictyostelium myosin II Kurzawa et al., 1997 >1000 s-1 for rabbit skeletal myosin II, Geeves andjeffries, 1988 100 s-1 for myosin lb at 20°C Coluccio and Geeves, 1999) and is accompanied by a very rapid... 

Millar, N. C., and Geeves, M. A. (1983). The limiting rate of the ATP-mediated dissociation of actin from rabbit skeletal muscle myosin subfragment 1. FEES Lett. 160, 141-148. 

Figure 7 Structures of calmodulin (blue) complexed to a peptide (yellow) from (a) CaMKK (1IQ5), (b) CaMKII (1CM1), (c) rabbit skeletal myosin light chain kinase (SLMK) (2BBM), and (d) glutamate decarboxylase (INWD) ...

Fig. 1. regulation of the superprecipitation of myosin B from rabbit skeletal... 

Abbreviations Ch.g., chicken gizzard T.g., turkey gizzard Rsk, rabbit skeletal muscle HMM, heavy meromyosin S-1, myosin subfrag-ment-1 TN, troponin. 

Unphosphorylated smooth muscle myosin does not move actin filaments, but does bind actin filaments and keep them associated with the coverslip surface (Umemoto and Sellers, 1990 Warshaw et al., 1990). Occasionally a few filaments can be observed to move over unphosphorylated myosin. As discussed in Chapter 1, this is consistent with the finding that phosphorylated and unphosphorylated smooth muscle HMM have fairly similar binding constants for actin in the presence of ATP (Sellers, 1985). Thus, the weakly bound unphosphorylated myosin heads are able to interact with actin sufficiently well to keep it bound to the surface. If unphosphorylated smooth muscle myosin is mixed in varying ratios with phosphorylated smooth muscle myosin, the rate of in vitro motility is decreased if the fraction of phosphorylated myosin is less than 50% (Warshaw et al., 1990). Unphosphorylated smooth muscle myosin, when mixed with rabbit skeletal muscle myosin, exerts an even more potent inhibitory effect on the rate of movement (Warshaw et al., 1990). Similar findings were also observed if mixtures of myosins are made on beads in the Nitella-hased motility assay (Sellers et al., 1985). 

Protein ( histidine ) Methyltransferase. An enzyme which methylates histidine in proteins to give primarily 3-methylhistidine residues has been observed in myofibrillar protein and in the sarcoplasmic fraction of muscle homogenates (218). S-Adenosyl-L-methionine serves as the methyl donor for the enzyme. The enzyme has not been solubilized and purified. Very little is known about the substrate specificity of protein-(histidine) methyltransferase. Actins from a wide variety of species consistently contain one 3-N-methylhistidine residue per molecule (191, 219). It appears that myosin from white muscle contains two residues of 3-N-methylhistidine (one residue per heavy chain), whereas myosin from red muscle contains no 3-N-methylhistidine (220). The amino acid sequence around the methylated residue of rabbit skeletal muscle is (221) ... 

The amino acid sequence in rabbit cardiac muscle myosin is homologous with that around the 3-N-methylhistidine residue in rabbit skeletal muscle myosin, yet it does not contain a 3-N-methylhistidine residue. 

Many systems of interest to the macromolecular chemist contain significant concentrations of only a few macromolecular species. In systems containing only two species it may be worthwhile to fit 7i(q, t) to two exponentials. This is especially so when the relative concentrations of the two species can be varied. Herbert and Carlson (1971) have, for instance, combined integrated intensity and spectral measurements to study the self-association of rabbit skeletal muscle myosin. 

Casimiro, D. R., Wong, L. L., Colon, J. L., Zewert, T. E., Richards, J. H., Chang, I-J., Winkler, J. R. and Gray, H. B, 1993, Electron transfer in ruthenium / zinc porphyrin derivatives of recombinant human myoglobins. Analysis of tunneling pathways in myoglobin and cytochrome c. Journal of American Chemical Society 115, 1485-1489. Chang, Y-C. and Ludescher, R. D, 1994, Local conformation of rabbit skeletal myosin rod filaments probed by intrinsic tryptophan fluorescence. Biochemistry 33, 2313 -2321. 

Preparation and Modification ofActin and Myosin from Rabbit Skeletal Muscle... 

Figure 12.9 Single moLecuLe studies can reveal enzyme kinetic information. Left the acto-myosin ATPase cycle lined up with a typical binding event the event begins when myosin binds to actin and ends when an ATP molecule diffuses into the binding cleft, causing it to dissociate from the actin filament. Right the event lifetimes of rabbit skeletal myosin-II SI fragment are stochastic and show an exponential distribution because each event is terminated by a single Poisson process (ATP binding). Note that the inset has two points removed, as zeros cannot be plotted on a log scale...

Lobley GE, Lovie JM (1979) The synthesis of myosin, actin and the major protein fractions in rabbit skeletal muscle. Biochem J 182 867-874... 

A study on rabbit skeletal myosin gave the total number of -SH groups... 

Spudich, J. A., and Watt, S. (1971). The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin. J. Biol. Chem. 246,4866-4871. 

Glycogen-debranching enzyme, a- and ) -subunits of phosphorylase kinase, glycogen phosphorylase, and glycogen synthase have been shown to be associated with the protein-glycogen complex isolated from rabbit skeletal muscle. Three other protein species, namely the heavy chains of myosin, actin, and calsequestrin, which were reported to be present in earlier preparations, have been shown to be constituents of particulate material which has co-precipitated with the protein-glycogen complex. 

Major progress continues to be reported in a number of extremely important areas. Among the muscle proteins, the complete sequence of rabbit skeletal muscle troponin T (259 residues) has been reported.The two forms of this protein from chicken breast and leg muscle differ in their A-terminal regions, the breast muscle enzyme carrying an extra 24 residues, rich in L-histidine and l-alanine. " Troponin I from a number of different sources has been studied. " Further structural studies on myosin light chains and actins from different sources have been reported. 

Among multitryptophan proteins emitting light around 330 nm, we have observed the largest red-edge effect (estimated from the difference between the maxima of the fluorescence spectra obtained at 290- and 305-nm excitation) for papain in the active and inactive forms (13 and 10 nm, respectively). Large shifts were also observed for rabbit muscle asparagyl- and valyl-RNA synthetases (8 nm). For rabbit aldolase A, the observed shift was 6 nm, for skeletal muscle myosin, 4.5 nm, for chymotrypsin, 2.5 nm, and for carbonic... 

Sreter, F. A., Seidel, J. C., and Gergely, J., Studies on myosin from red and white skeletal muscles of the rabbit. I. Adenosine triphosphatase activity. J. Biol. Chem. 241, 5772-5776 (1966). 

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