PubMed · 6964537
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E Edorigo. [Composites: a cyclic evaluation].. https://pubmed.ncbi.nlm.nih.gov/6964537/
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The self-association of recombinant human interleukin-2 (rhIL-2) in solution was investigated as a function of pH and temperature using equilibrium sedimentation. Studies were performed at pH 3.6, 6.5 and 8.2, at 1 degree C and 20 degrees C. A model assuming an ideal single molecular species describes the data observed at pH 6.5 at both temperatures. At pH 8.2, the data from both temperatures can be better described by a weak monomer-dimer association equilibrium. The values of the association constants obtained indicate the presence of less than 10% dimer at a concentration of 1 mg/ml at both temperatures. At pH 3.6, aggregates with a Z average molecular weight of over 35 times that of monomeric rhIL-2 were formed. The smallest associating species present under these conditions corresponds to the monomer, which produces aggregates with a wide range of molecular weights. The monomer appears to be in equilibrium with the smallest aggregates, in that a model describing an indefinite association fits the data obtained at the highest centrifugal speed. No model was found to successfully describe the association of the monomer into the much larger aggregates observed at lower speeds. This may be the result of the lack of rapid thermodynamic reversibility of the larger aggregates. Temperature was found to have no significant effect on the largest aggregates that were formed at pH 3.6.
The UV-visible absorption spectra and photostationary state compositions of retinal (or the related C-18 ketone, 3-dehydroretinal and the C-22 aldehyde) imbedded in the binding cavity of beta-lactoglobulin (BLG) are consistent with the view that the carbonyl group of these polyenes are hydrogen-bonded with the protein host, most likely with the lone protonated lysine residue in the binding pocket. Patterns of variation in photochemical behavior of the imbedded chromophore versus that in solution are discussed in terms of possible specific protein-substrate interactions. The results are also compared with that of the methyl ether of retinol where similar hydrogen bonding is not possible.
Molsidomine drugs corvaton and sidnopharm were assessed clinically, physicochemically and experimentally. Corvaton tablets contained more active substance but less cleavage products than sidnopharm ones. In experiment with acute transitory coronary insufficiency corvaton was active both during myocardial ischemia and in reperfusion. Corvaton showed antianginal effect in 70.3%, sidnopharm in 58.6% of cases. Both drugs produced a positive action on coronary and myocardial reserves in coronary patients with angina class I-III but did not affect hemodynamics. Oral sidnopharm induced side effects 4 times more frequently than corvaton. Corvaton tablets (single dose) activity lasted more than sidnopharm effect by 2.2 hours. Oral corvaton remained active 5.3 hours longer than the same intravenous dose.