Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)


Mol Pharmacol 1976 Mar
PMID:Inhibition of isoproterenol activation of adenylate cyclase by metoprolol, oxprenolol, and the para isomer of oxprenolol. 0 23


Mol Pharmacol 1976 Mar
PMID:Comparison of the effects of neuroleptic drugs on pre- and postsynaptic dopaminergic mechanisms in the rat striatum. 0 24


Mol Pharmacol 1976 Mar
PMID:Reduction of tertiary amine N-oxides by liver microsomal cytochrome P-450. 0 25


Mol Pharmacol 1976 Mar
PMID:An agonist-specific effect of guanine nucleotides on binding to the beta adrenergic receptor. 0 26

The dark and light reduction of nitrate and nitrite by cell-free preparations of the blue-green alga Anacystis nidulans has been investigated. The three following methods have been successfully applied to the preparation of active particulate fractions from the alga cells: (a) shaking with glass beads, (b) lysozyme treatment and lysis of the resulting protoplasts, and (c) sonication. The two enzymes of the nitrate-reducing system-namely, nitrate reductase and nitrite reductase-are firmly bound to the isolated pigment-containing particles, and can be easily solubilized by prolonging the vibration or sonication time. Both enzymes-whether solubilized or bound to the particles-depend on reduced ferredoxin as the immediate electron donor. In its presence, the alga particles catalyze the gradual photoreduction of nitrate to nitrite and ammonia, a process that can thus be considered as one of the most simple and relevant examples of Photosynthesis. Some of the properties of nitrate reductase have been studied. Nitrate reductase as well as nitrite reductase are adaptive enzymes repressed by ammonia.
Mol Cell Biochem 1976 Feb 25
PMID:Ferredoxin-dependent photosynthetic reduction of nitrate and nitrite by particles of Anacystis nidulans. 0 27


J Mol Biol 1976 Apr 05
PMID:Catalytic implications of electrostatic potentials: the lytic activity of lysozymes as a model. 0 9


J Mol Biol 1976 Apr 15
PMID:The charge-relay system of serine proteinases: proton magnetic resonance titration studies of the four histidines of porcine trypsin. 0 10

A simple method of two-dimensional polyacrylamide gel electrophoresis is described which affords: (1) high resolution of eukaryotic ribosomal proteins; (2) good recovery of protein in the transfer from first to second dimension; and (3) characterisation of the separated proteins in terms of molecular weights and other electrophoretic properties. Using this method, we have characterised 70 proteins in rabbit reticulocyte ribosomes, 30 from the small subunit and 40 from the large subunit. The molecular weight distribution is compared with those obtained by other authors after fractionation of the proteins in two dimensions.
Mol Gen Genet 1976 Dec 31
PMID:Characterisation of eukaryotic ribosomal proteins. 0 65

Proteins of yeast cytoplasmic ribosomes were analyzed by two different methods of two dimensional gel electrophoresis: run at pH 8.6 in 1-D1 and at pH 4.6 in 2-D (Method A); run at pH 5.0 in 1-D and in the presence of sodium dodecyl sulfate in 2-D (Method B). The numbers of proteins estimated were 28 (Method A) and 29 or 30 (Method B) in the 40S small subunit, and 40 (Method A) and 41 (Method B) in the 60S large subunit, respectively. Molecular weights of proteins in the small and the large subunits were found to be less than 40,000 and 60,000 respectively.
Mol Gen Genet 1976 Apr 23
PMID:Study on proteins from yeast cytoplasmic ribosomes by two-dimensional gel electrophoresis. 0 66

1. The thermodynamics and molecular basis of energy-linked conformational changes in the cytochrome aa3 and ATP synthetase complexes of the mitochondrial membrane have been studied with spectrophotometrical and fluorometrical techniques. 2. Ferric cytochrome aa3 exists in two conformations, high spin and low spin, the equilibrium between these states being controlled by the electrical potential difference across the mitochondrial membrane. The conformational change is brought about by an electrical field-driven binding of one proton per aa3 to the complex. At pH 7.2 the concentration of the two conformations is equal at a membrane potential of 170 mV corresponding to about 4 kcal/mole. 3. The high to low spin transition in ferric aa3 is also induced by hydrolysis of ATP in which case two molecules of aa3 are shifted per ATP molecule hydrolyzed. This is in accordance with translocation of two protons across the mitochondrial membrane coupled to hydrolysis of ATP as proposed in the chemiosmotic theory of oxidative phosphorylation. 4. The conformational transition in cytochrome aa3 is not an expression of the formation of a 'high-energy' intermediate or reversal of the energy-transducing pathway of oxidative phosphorylation, but is presumably the basis of allosteric control of the activity of cytochrome oxidase by the energy state of the mitochondrion. This control is exerted by a regulatory mechanism in which the electrical potential difference controls the conformation and redox properties of the heme centres and thereby the rate of oxygen consumption. 5. The synthesis of one molecule of ATP by oxidative phosphorylation is energetically equivalent to the work done in carrying two electrical charges across the entire mitochondrial membrane. 6. Fluorescence changes of aurovertin bound to ATP synthetase reveal that the electrical membrane potential induces a conformational change in the F1 portion of the enzyme which is probably associated with dissociation of the natural F1 inhibitor protein. This conformational change is energetically equivalent to the work done in carrying one electrical charge across the mitochondrial membrane. 7. A model is proposed for the mechanism of the electrical field-induced conformational changes in the cytochrome aa3 and ATP synthetase complexes, and the significance of these changes in the mechanism and control of mitochondrial energy conservation is discussed.
Mol Cell Biochem 1976 Mar 26
PMID:Conformational changes in cytochrome aa3 and ATP synthetase of the mitochondrial membrane and their role in mitochondrial energy transduction. 0 67


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