Of Rabbit Skeletal Muscle

Sygusch, J., Beaudry, D., Allaire, M. Molecular architecture of rabbit skeletal muscle aldolase at 2.7 A resolution. Proe. Natl. Aead. Sei. USA 84 ... 

Myofibrillar Structural Proteins of Rabbit Skeletal Muscle ... 

Louis, C.F., Saunders, M.J., and Holroyd, J.A. (1977) The cross-linking of rabbit skeletal muscle sarcoplasmic reticulum protein. Biochim. Biophys. Acta 493, 78-92. 

Tsuda, S., Ogura, K., Hasegawa, Y., Vagi, K., and Hikichi, K. (1990). H NMR study of rabbit skeletal muscle troponin C Mgf -Induced conformational change. Biochemistry 29, 4951-4958. 

Purich, D.L. Fromm, H.J. Inhibition of rabbit skeletal muscle adenylate kinase by the transition state analogue, P P -di(adenosine-5 )tetraphos-phate. Biochim. Biophys. Acta, 276, 563-567 (1972)... 

Collins, J. H., Potter, J. D., Horn, M. C. J., Wilshire, G., and Jackman, N. The amino acid sequence of rabbit skeletal muscle troponinC Gene replication and homology with calciumbinding proteins from carp and hake muscle. FEBS Letters 36, 268—272 (1973). 

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). 

Pearlstone, J. R., and Smillie, L. B. (1985). The interaction of rabbit skeletal muscle troponin-T fragments with troponin-I. Can.]. Biochem. Cell. Biol. 63, 212-218. 

Sano, K.-I., Maeda, K., Oda, T., and Maeda, Y. (2000). The effect of single residue substitutions of serine-283 on the strength of head-to-tail interaction and actin binding properties of rabbit skeletal muscle a-tropomyosin. /. Biochem. 127, 1095-1102. 

Parmeggiani A, Luft JH, Love DS, Krebs EG (1966), Crystallization and properties of rabbit skeletal muscle phosphofructokinase, J. Biol. Chem. 241 4625-4637. 

Bock, P.E., and C. Frieden (1974). pH-induced cold lability of rabbit skeletal muscle phosphofructoki-nase. Biochemistry 13 4191-4196. 

Carter. J.. and Smith. E. E. 1978. Actions of glycogen synthase and phosphorylase of rabbit-skeletal muscle on modified glycogens. Carbohydr. Res. 61, 395-406. 

Pitcher, J., Smythe, C., Campbell, D. G., and Cohen, P. 1987. Identification of the 38-kDa subunit of rabbit skeletal muscle glycogen synthase as gtycogenin. Eur. J. Biochem. 169,497-502. 

Crystallized Enzymes from the Myogen of Rabbit Skeletal Muscle R. Czok and Th. Bucher... 

Czok, R., and Buecher, T. 1960. Crystallized enzymes from the myogen of rabbit skeletal muscle. Adv. Protein Chem. 15 315-415. 

On separated thin filaments of rabbit skeletal muscle, anti-troponin T1 formed a relatively wide striation at the same position as in the case of chicken skeletal muscle. The Fab fragment of the antibody formed a narrow striation at a position corresponding to the top side of the filament of the wide striation formed by y-globulin (1. Ohtsuki, unpublished results). This is consistent with the latter explanation at least for the orientation of the antigenic regions in troponin Ti. A possible arrangement of troponin Ti and T2 regions in the thin filament is shown in Fig. 10. 

G9. Golisch, G., Pette, D., and Piehlmeyer, H., Metabolic differentiation of rabbit skeletal muscle as induced by specific innervation. Eur. J. Biochem. 16, 110-116 (1970). 

It shows considerable inhibition of cAMP-phosphodiesterase in rat adipose tissues and inhibits non-enzymic lipid peroxidation. It is a potent scavenger of superoxide and increases the beat rate on isolated atria, stimulates lipolysis and causes a concentration-dependent increase in Ca release from the heavy fraction of fragmented sarcoplasmic reticulum of rabbit skeletal muscle. ... 

Crystallisation was used for many years as a step in the isolation and purification of proteins. Microcrystallinity (the appearance of a silky sheen) was one of the first indications of approaching purity. A good early review of protein crystallisation stemming from this tradition is given by Czok and Bucher [29] for the enzymes of rabbit skeletal muscle. In the past, proteins selected for study were those that were readily available and crystallisable. It is noteworthy that a large number of the enzymes illustrated in Dixon and Webb s [30] crystal atlas have now had their structure solved by X-ray diffraction. 

Heilmeyer, L. M. J., Serwe, M., Weber, C., Metzger, J., Hoffmann-Posorske, E., Meyer, H. E. (1993). Famesyl cysteine is a constituent of the alpha and beta subunits of rabbit skeletal muscle phosphorylase kinase. Proc. Natl. Acad. Sci. USA 89,9554-9558. 

Domain 3 stretches from amino acids 463 (432) to 645 (589) and corresponds to exons 5, 6, and 7. The core of domain 3 is again a single a-helix stabilized by intrahelix salt bridges. The sequence from 565 (509) to 621 (565) is 43% identical to the amino acids 90-146 of rabbit skeletal muscle troponin T, which is a TM binding site in troponin T. Domain 4 stretches from 646 (590) to the C terminus and corresponds to exons 8-13. This is an extended and stably folded region that contains little regular secondary structure (Levine et al.,... 

PPl enzymatic forms are present in the cytosolic and particulate fractions of the cell. PPl was purified from the cytosolic fraction of rabbit skeletal muscle in an inactive form and called the MgATP-dependent phosphatase, since it could be activated by incubation with MgATP plus a protein factor identified later as glycogen synthase kinase-3 (Bollen and Stalmans,... 

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) ... 

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. 

Chevallier j and Butow RA (1971) Calcium binding to the sarcoplasmic reticulum of rabbit skeletal muscle. Biochemistry 10 2733-2737. 

Persson, M. G., Gustafsson, L. E., Wiklund, N., Hedqvist, P., and Moncada, S. (1990). Endogenous nitric oxide as a modulator of rabbit skeletal muscle microcirculation in vivo. Br. J. Pharmacol. 100, 463-466. 

Krebs, E.G. Fischer, E.H. Phosphorylase b-to-a converting enzyme of rabbit skeletal muscle. Biochim. Biophys. Acta, 20, 150-157 (1956)... 

Hayakawa, T. Perkins, J.P. Walsh, D.A. Krebs, E.G. Physiochemical properties of rabbit skeletal muscle phosphorylase kinase. Biochemistry, 12, 567-573 (1973)... 

Cohen, R Burchell, A. Foulkes, J.G. Cohen, P.T.W. Vanaman, T.C. Nairn, A.C. Identification of the Ca -dependent modulator protein as the fourth subunit of rabbit skeletal muscle phosphorylase kinase. FEBS Lett., 92, 287-293 (1978)... 

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