Purification and Partial Characterization of Cardiac Plasma Membranes Rich in Beta-Adrenoreceptors

References

• Stam A. C., Jr., et al. A myocardial sarcolemma preparation and the ouabain-sensitive (Na+ K+)-ATPase. Biochem. Biophys. Acta 1969; 189: 304307
   Google Scholar
• Stam A. C., Jr., et al. Canine myocardial sarcolemma–its preparation and enzymatic activity. J. Mol. Cell. Cardial. 1970; 1: 117–130
   Google Scholar
• Kidwai A. W., et al. Isolation of plasma membrane from cardiac muscle. Biochem. Biophys. Res. Comm. 1971; 45: 901–910
   Google Scholar
• Tada M., et al. Preparation and properties of plasma membranes from guinea pig hearts. J. Mol. Cell. Cardiol. 1972; 4: 417–426
   Google Scholar
• Saccomani G., et al. Preparation and characterization of plasma membrane of cardiac tissue. J. Mol. Cell. Cardiol. 1974; 6: 505–521
   Google Scholar
• Jarrott B., Picken G. Cardiac adenylate cyclase. I. Preparation and characterization of a subcellular fraction containing catechola-mine-sensitive adenylate cyclase. J. Mol. Cell. Cardiol. 1975; 7: 685–695
   Google Scholar
• St Louis P. J., Sulakhe P. V. Isolation of sarcolemmal membranes from cardiac muscle. Int. J. Biochem. 1976; 7: 547–558
   Google Scholar
• Bloomfield F. J., et al. Analytical subcellular fractionation of guinea pig myocardium. Clin. Sci. and Mol. Med. 1977; 63: 63–74
   Google Scholar
• McNamara D. B., et al. Properties of heart sarcolemmal Na+-K+ ATPase. J. Biochem. 1974; 75: 795–803
   PubMed Web of Science ®Google Scholar
• Besch H. R., Jr., Jones L. R., Watanabe A. M. Intact vesicles of canine cardiac sarcolemma. Evidence from vectorial properties of Na+ K+-ATPase. Cir. Res. 1976; 39: 586–595
   PubMed Web of Science ®Google Scholar
• Jones L. R., et al. Separation of vesicles of cardiac sarcolemma from vesicles of cardiac sarcoplasmic reticulum. Comparative biochemical analysis of component activities. J. Biol. Chem. 1979; 254: 530–539
   PubMed Web of Science ®Google Scholar
• Pitts B. J. R., Swartz A. Improved purification and partial characterization of (Na+ K+)-ATPase from cardial muscle. Biochim. Biophys. Acta 1975; 401: 184–195
   Google Scholar
• Katchalski A., et al. Interactions of basic polyelectrolytes with the red blood cell. II. Agglutination of red blood cells by polymeric bases. Biochim. Biophys. Acta 1959; 33: 120–138
   Google Scholar
• Brossmer R., Pfleiderer T. On the mechanism of thrombocyte aggregation. I. The effect of the change of high molecular weight substances on aggregation in vitro with special reference to dextran derivatives. Naturwissenschaften 1966; 53: 464–466
   Google Scholar
• Dangerfield W. G., Faulkner G. Estimation of serum lipoproteins using sulphated polysaccharides. Clin. Chim. Acta 1964; 10: 123–133
   Google Scholar
• Philipson L., Kaufman M. The efficiency of ribonuclease inhibitors tested with viral ribonucleic acid as substrate. Biochim. Biophys. Acta 1964; 80: 151–154
   Google Scholar
• Bornens M., Courvalin J.-C. Isolation of nuclear envelopes with polyanions. J. Cell. Biol. 1978; 76: 191–206
   Google Scholar
• Wheeldon L. W., Gan K. Resolution of fragments of plasma and sarcotubular membranes in heart muscle microsomes. Biochim. Biophys. Acta 1971; 233: 37–48
   Google Scholar
• Maguire M. E., Ross E. M., Gilman A. G. β-adrenergic receptor: Ligand binding properties and the interaction with adenylyl cyclase. Adv. Cyclic. Nucl. Res. 1977; 8: 1–83
   PubMedGoogle Scholar
• Wolfe B. B., Harden T. K., Molinoff P. B. In vitro study of (3-adrenergic receptors. Ann. Rev. Pharmacol. Toxicol. 1977; 17: 575–604
   PubMed Web of Science ®Google Scholar
• Levitzki A. Catecholamine receptors. Rev. Physiol. Biochem. Pharmacol. 1978; 82: 1–26
   PubMedGoogle Scholar
• Baker S. P., Boyd H., Potter L. T. Distribution and function of β-adrenoceptors in different chambers of the canine heart. Br. J. Pharmacol. 1980; 68: 57–63
   PubMed Web of Science ®Google Scholar
• Gelbart A., Goldman R. H. Correlation between microsomal (Na+ K+)-ATPase activity and [3H] ouabain binding to heart tissue homogenates. Biochim. Biophys. Acta 1977; 481: 689–694
   Google Scholar
• Ramachandran J. A new simple method for separation of adenosine 3′, 5′-cyclic monophosphate from other nucleotides and its use in the assay of adenyl cyclase. Anal. Biochem. 1971; 43: 227–239
   PubMed Web of Science ®Google Scholar
• Gentry M. K., Olsson R. A. A simple, specific, radioisotopic assay for 5′-nucleotidase. Anal. Biochem. 1975; 64: 624–627
   Google Scholar
• Baker S. P., Hemsworth B. A. Effect of mitochondrial lipid peroxidation on monoamine oxidase. Biochem. Pharmacol. 1978; 27: 805–806
   Google Scholar
• Pennington R. J. Biochemistry of dystrophic muscle. Mitochondrial succinate-tetrazolium reductase and adenosine triphosphatase. Biochem. J. 1961; 80: 649–654
   PubMed Web of Science ®Google Scholar
• Hubscher G., West G. R. Specific assays of some phosphatases in subcellular fractions of small intestinal mucosa. Nature 1965; 205: 799–800
   PubMed Web of Science ®Google Scholar
• Fiske C. H., Subbarow Y. The colorimetric determination of phosphorus. J Biol. Chem. 1975; 66: 375–400
   Google Scholar
• Lowry O. H., et al. Protein measurement with the Folin phenol reagent. J. Biol. Chem. 1951; 193: 265–275
   PubMed Web of Science ®Google Scholar
• Bradford M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of proteindye binding. Anal. Biochem. 1976; 72: 248–254
   PubMed Web of Science ®Google Scholar
• Zahler W. L. Analytical polyacrylamide gel electrophoresis and molecular weight determinations. Methods in Enzymol. 1974; 32: 70–82, Part B
   Google Scholar
• Hinton R. H., Reid E. Enzyme distribution in mammalian membranes. Mammalian Cell Membranes, G. A. Jamieson, D. M. Robinson. Butterworths, Boston 1976; vol. 1: 161–197
   Google Scholar
• Hatefi Y., Hanstein W. G. Destabilization of membranes with chaotropic ions. Methods in Enzymol. 1974; 31: 770–790, Part A
   PubMedGoogle Scholar
• Sanders R. B., Thompson W. J., Robison G. A. Epinephrine and glucagon-stimulated cardiac adenylyl cyclase activity. Biochim. Biophys. Acta 1977; 498: 10–20
   PubMedGoogle Scholar
• Katz M. S., et al. Activation of epinephrine and glucagon-sensitive adenylate cyclase of rat liver by cytosol protein factors. Role in loss of enzyme activities during preparation of particulate fractions, quantitation and partial characterization. J. Cyclic Nucleo. Res. 1978; 5: 389–407
   Google Scholar
• Lau Y. H., Caswell A. H., Brunschwig J.-P. Isolation of transverse tubules by fractionation of triad junctions of skeletal muscle. J. Biol. Chem. 1977; 252: 5565–5574
   PubMed Web of Science ®Google Scholar
• Toda G., et al. Subfractionation of rat liver plasma membrane. Uneven distribution of plasma membrane-bound enzymes on the liver cell surface. Biochim. Biophys. Acta 1975; 413: 52–64
   Google Scholar