Membrane ATPase of Escherichia coli K 12. Selective solubilization of the enzyme and its stimulation by trypsin in the soluble and membrane-bound states.

[1]  B. Simon,et al.  HCO 3 -stimulated ATPase from mammalian pancreas. Properties and its arrangement with other enzyme activities. , 1972, Biochimica et biophysica acta.

[2]  M. Schor,et al.  Subunit structure and properties of two forms of adenosine triphosphatase released from Micrococcus lysodeikticus membranes. , 1972, Biochemical and biophysical research communications.

[3]  I. A. Siegel,et al.  A microsomal HCO 2 -stimulated ATPase from the dog submandibular gland. , 1972, Biochimica et biophysica acta.

[4]  M. Roisin,et al.  The membrane ATPase of Escherichia coli. I. Ion dependence and ATP-ADP exchange reaction. , 1972, Biochimica et biophysica acta.

[5]  G. Sachs,et al.  Properties of ATPase of gastric mucosa. 3. Distribution of HCO 3 -stimulated ATPase in gastric mucosa. , 1972, Biochimica et biophysica acta.

[6]  P. Davies,et al.  Properties of a soluble Ca 2+ - and Mg 2+ -activated ATPase released from Escherichia coli membranes. , 1972, Biochimica et biophysica acta.

[7]  E. Muñoz,et al.  Properties of the membrane—adenosine triphosphatase complex ofMicrococcus lysodeikticus: Reversibility of the Mg2+‐dependent states of the ATPase , 1972, FEBS letters.

[8]  V. Barlow,et al.  Purification and properties of ATPase from the cytoplasmic membrane of Bacillus megaterium KM. , 1971, Biochimica et biophysica acta.

[9]  D. Wallach,et al.  Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane. , 1971, Biochemistry.

[10]  E. Muñoz,et al.  Dependence on Mg2+ for different states of the membrane‐bound adenosine triphosphatase of Micrococcus lysodeikticus , 1971, FEBS letters.

[11]  D. Evans.  Membrane Mg2+-(Ca2+)-Activated Adenosine Triphosphatase of Escherichia coli: Characterization in the Membrane-Bound and Solubilized States , 1970, Journal of bacteriology.

[12]  A. Abrams,et al.  Membrane adenosine triphosphatase from Streptococcus faecalis. Preparation and homogeneity. , 1970, The Journal of biological chemistry.

[13]  D. Evans.  Membrane Adenosine Triphosphatase of Escherichia coli: Activation by Calcium Ion and Inhibition by Monovalent Cations , 1969, Journal of bacteriology.

[14]  S. Mizushima,et al.  The membrane ATPase of Bacillus megaterium. II. Purification of membrane ATPases and their recombination with membrane. , 1969, Journal of biochemistry.

[15]  M. Schor,et al.  Adenosinetriphosphatase of Micrococcus lysodeikticus: selective release and relationship to membrane structure. , 1968, Biochemical and biophysical research communications.

[16]  Kaback Hr.  The Role of the Phosphoenolpyruvate-phosphotransferase System in the Transport of Sugars by Isolated Membrane Preparations of Escherichia coli , 1968 .

[17]  C. Baron,et al.  The isolation and subunit structure of streptococcal membrane adenosine triphosphatase. , 1967, Biochemistry.

[18]  G. Weinbaum,et al.  A rapid technique for distinguishing enzymatically active proteins in the cell"envelope" of Escherichia coli B. , 1966, Biochimica et biophysica acta.

[19]  H. Determann,et al.  The correlation between molecular weight and elution behaviour in the gel chromatography of proteins , 1966 .

[20]  E. Racker,et al.  PARTIAL RESOLUTION OF THE ENZYMES CATALYZINE PHOTOPHOSPHORYLATION. I. STIMULATION OF PHOTOPHOSPHORYLATION BY A PREPARATION OF A LATENT, CA++- DEPENDENT ADENOSINE TRIPHOSPHATASE FROM CHLOROPLASTS. , 1965, The Journal of biological chemistry.

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