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Results: 791 to 795 of 795

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Effect of oxygen concentration on trasverse water proton relaxation times in erythrocytes homozygous and heterozygous for hemoglonin S.
Cottam GL, Waterman MR
(1976) Arch Biochem Biophys 177: 293-8
MeSH Terms: Electron Spin Resonance Spectroscopy, Hemoglobin, Sickle, Hemoglobins, Heterozygote, Homozygote, Humans, Hydrogen Bonding, Kinetics, Mathematics, Oxygen, Oxyhemoglobins, Protein Binding, Protein Conformation, Water
Added February 12, 2015
0 Communities
1 Members
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14 MeSH Terms
Effect of carbamidomethylation of cysteine residues G11(104)alpha on the properties of hemoglobin A.
Waterman MR
(1976) Biochim Biophys Acta 439: 167-74
MeSH Terms: Binding Sites, Cysteine, Electron Spin Resonance Spectroscopy, Electrophoresis, Disc, Hemoglobins, Humans, Iodoacetamide, Macromolecular Substances, Oxygen, Oxyhemoglobins, Protein Binding, Protein Conformation
Show Abstract · Added February 12, 2015
A modified hemoglobin tetramer has been prepared containing carbamidomethylated G11(104)alpha cysteine residues. The molecule is electrophoretically identical to hemoglobin A, at pH 8.6, contains 2 titratable sulfhydryl groups per tetramer, and shows a normal oxygen affinity at half-saturation. However, the cooperative oxygen binding is significantly decreased. As the G11(104)alpha cysteine residues are located at the alpha1beta1 contact point in the hemoglobin tetramer, the results of this study indicate that modification within this portion of the molecule does not interfere with the assembly of subunits to form a tetramer or the resultant p50 but can cause a significant alteration of cooperative oxygen binding. In addition, spin-labels attached to this cysteine residue are not sensitive to changes in conformation which may take place at this contact point during oxygen binding. It is therefore possible that modification of the G11(104)alpha cysteine residue abolishes the contribution of the alpha1beta1 contact point to the cooperative oxygen binding phenomenon.
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12 MeSH Terms
Site-specific anti-cytochrome c antibodies. Inhibition of the reactions between cytochrome c and its respiratory chain electron exchange partners.
Osheroff N, Jemmerson R, Speck SH, Ferguson-Miller S, Margoliash E
(1979) J Biol Chem 254: 12717-24
MeSH Terms: Animals, Antibodies, Antigen-Antibody Complex, Binding Sites, Antibody, Cytochrome c Group, Electron Transport, Epitopes, Horses, Immunoglobulin Fab Fragments, Kinetics, Models, Molecular, Protein Conformation, Rabbits
Added March 5, 2014
0 Communities
1 Members
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13 MeSH Terms
Nitric oxide induced conformational changes in opossum hemoglobin.
John ME, Waterman MR
(1979) J Biol Chem 254: 11953-7
MeSH Terms: Amino Acids, Animals, Electron Spin Resonance Spectroscopy, Hemoglobin A, Hemoglobins, Humans, Hydrogen-Ion Concentration, Kinetics, Nitric Oxide, Opossums, Oxyhemoglobins, Protein Binding, Protein Conformation, Species Specificity
Show Abstract · Added February 12, 2015
Opossum hemoglobin assumes a T quaternary structure upon NO ligation in the absence of organic phophates at pH 6.7. In addition, stripped opossum hemoglobin exhibits a low oxygen affinity when compared to human hemoglobin and a pH-dependent heme-heme interaction with an n value of 2.14 at pH 7.0 and 2.46 at pH 7.35. These observations indicate that opossum hemoglobin may have a destabilized oxy structure when compared to hemoglobin A due to differences in primary structure. Thus, the strong trans ligand effect of nitric oxide is able to disrupt the proximal histidine-iron bond in the alpha-hemes triggering a conformational transition to the T state. Absence of a distal histidine in the alpha-subunits and, therefore an impaired donor acceptor interaction with the sixth ligand, could contribute to the lack of stability of the R quaternary structure in opossum nitrosylhemoglobin. The reduced oxygen affinity of opossum hemoglobin may be compensated for by other physiological factors such as a reduced phosphate effect.
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14 MeSH Terms
Phosphofructokinase. II. Role of ligands in pH-dependent structural changes of the rabbit muscle enzyme.
Bock PE, Frieden C
(1976) J Biol Chem 251: 5637-43
MeSH Terms: Adenosine Triphosphate, Animals, Binding Sites, Enzyme Activation, Hydrogen-Ion Concentration, Inosine Nucleotides, Kinetics, Ligands, Magnesium, Muscles, Phosphofructokinase-1, Protein Binding, Protein Conformation, Rabbits
Show Abstract · Added January 20, 2015
The effect of ligands, including substrates and allosteric effectors, on the pH-dependent inactivation and reactivation of rabbit muscle phosphofructokinase has been examined in terms of the mechanism proposed previously (Bock, P.E. and Fireden, C. (1976) J. Biol. Chem. 251, 5630-5636). It is concluded thatt many ligands exert their effect by binding preferentially to either protonated or unprotonated forms of the enzyme and thus shifting an apparent pK for the inactivation or reactivation process. ATP and fructose 6-phosphate influence the apparent pK to different extents and in different directions, with ATP binding preferentially to the protonated forms and fructose 6-phosphate to the unprotonated forms. Enzyme inactivated by ATP can be reactivated by the addition of fructose 6-phosphate. The experiments indicate that inactivation and reactivation in the presence of these ligands can occur by kinetically different pathways as has been found for these processes in the absence of ligands. The results are discussed in relation to what might be expected for ligand binding properties of the enzyme as a function of pH, temperature, and enzyme concentration. The effect of ATP and MgATP is complex, perhaps representing more than one site of binding. Citrate appears to bind preferentially to protonated forms of the enzyme while fructose 1,6-bisphosphate and AMP bind preferentially to the unprotonated forms. ADP, K+, and NH4+ appear to have little or no preference in binding to different enzyme forms.
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14 MeSH Terms