The association of human erythrocyte catalase with the cell membrane.

[1]  M. Palcic,et al.  The reaction of human erythrocyte catalase with hydroperoxides to form compound I. , 1980, The Journal of biological chemistry.

[2]  D. R. Yeltman,et al.  Localization and membrane association of aldolase in human erythrocytes. , 1980, Archives of biochemistry and biophysics.

[3]  C. Howe,et al.  Peripheral proteins of human erythrocytes. , 1978, Biochemical and biophysical research communications.

[4]  J. Yguerabide,et al.  Classification and localization of hemoglobin binding sites on the red blood cell membrane. , 1977, Biochemistry.

[5]  J. Yguerabide,et al.  Interaction of hemoglobin with red blood cell membranes as shown by a fluorescent chromophore. , 1977, Biochemistry.

[6]  S. Srivastava,et al.  Partition of catalase and its peroxidase activities in human red cell membrane: effect of ATP depletion. , 1977, Biochimica et biophysica acta.

[7]  S. Damgaard Tritium effect in peroxidation of ehtanol by liver catalase. , 1977, Biochemical Journal.

[8]  T. Steck,et al.  Interaction of the aldolase and the membrane of human erythrocytes. , 1977, Biochemistry.

[9]  T. Steck,et al.  Binding of rabbit muscle aldolase to band 3, the predominant polypeptide of the human erythrocyte membrane. , 1976, Biochemistry.

[10]  M. L. Kremer Kinetics of reduction of the catalase-hydrogen peroxide complex by ethanol , 1975 .

[11]  T. Steck THE ORGANIZATION OF PROTEINS IN THE HUMAN RED BLOOD CELL MEMBRANE , 1974, The Journal of cell biology.

[12]  I. Fridovich,et al.  Visualization of catalase on acrylamide gels. , 1974, Analytical biochemistry.

[13]  T. Steck,et al.  Specificity in the association of glyceraldehyde 3-phosphate dehydrogenase with isolated human erythrocyte membranes. , 1973, The Journal of biological chemistry.

[14]  T. Steck,et al.  Selective solubilization of proteins and phospholipids from red blood cell membranes by nonionic detergents. , 1973, Journal of supramolecular structure.

[15]  J. Bonaventura,et al.  Human erythrocyte catalase: an improved method of isolation and a reevaluation of reported properties. , 1972, Archives of biochemistry and biophysics.

[16]  J. von Wartburg,et al.  Heterogeneity of erythrocyte catalase. Correlations between sulfhydryl group content, chromatographic and electrophoretic properties. , 1969, European journal of biochemistry.

[17]  P. Nicholls,et al.  ACTIVITY OF CATALASE IN THE RED CELL. , 1965, Biochimica et biophysica acta.

[18]  P. Howard,et al.  Human Erythrocyte Catalase: Demonstration of Heterogeneity and Relationship to Erythrocyte Ageing in vivo , 1964, British journal of haematology.

[19]  J. Donovan THE SPECTROPHOTOMETRIC TITRATION OF THE SULFHYDRYL AND PHENOLIC GROUPS OF ALDOLASE. , 1964, Biochemistry.

[20]  J. Dodge,et al.  The preparation and chemical characteristics of hemoglobin-free ghosts of human erythrocytes. , 1963, Archives of biochemistry and biophysics.

[21]  Dandliker Wb,et al.  The coenzyme content of rabbit muscle D-glyceraldehyde-3-phosphate dehydrogenase. , 1956 .

[22]  R. F. Beers,et al.  Progressive inhibition of the catalase-hydrogen peroxide system by acetate, chloride and azide. , 1956, Archives of biochemistry and biophysics.

[23]  O. H. Lowry,et al.  Protein measurement with the Folin phenol reagent. , 1951, The Journal of biological chemistry.