PubMed Health⌕ Search

Biomedical subjects

R S Rapaka

Publications and source records attributed to R S Rapaka.

At least 37 records · Page 2Linked to original sources
PubMed1986

Preliminary studies of the secondary structure in solution of two phosphoproteins of chicken bone matrix by circular dichroism and fourier transform-infrared spectroscopy.

The secondary structures of two phosphoproteins from chicken bone matrix of Mr approximately 15kDa and approximately 28kDa, rich in Asx, Glx, and Ser, and containing Ser(P) and Thr(P) residues, have been investigated in solution by Circular Dichroism (CD) and Fourier Transform-Infrared Spectroscopy (FT-IR). CD spectroscopy, which yields useful information on the backbone conformation of polypeptides and proteins, suggests a predominantly beta-sheet structure for the two phosphoproteins. The FT-IR spectra of the approximately 15kDa protein, which is sensitive to secondary structure and hence provides complimentary information to CD spectroscopy, are consistent with the results obtained by CD studies.

Amino Acids↗
PubMed1986

Molecular mechanisms of ligand binding to opioid receptors: selective inhibition by ethanol?

Effects of varying concentrations of ethanol on the conformations of DAGO, a mu-specific opioid ligand were monitored by FT-IR spectroscopy. The binding of 3H-labeled DAGO (mu-agonist) and DSLET (delta-agonist) to opioid receptors in the presence of varying concentrations of alcohol was also determined. The results indicate that the conformational features of the ligands are altered and conformational factors may play a role in ligand-receptor interaction.

Animals↗
PubMed1985

Conformational states of Leu5- and Met5-enkephalins in solution.

The molecular conformations of Leu5- and Met5-enkephalins in aqueous and DMSO solutions were investigated by FT-IR and laser Raman spectroscopic methods. The amide I, II, and III regions in the FT-IR spectra of Leu5- and Met5-enkephalins in aqueous solution were analyzed by performing Fourier self-deconvolution of the bands. Leu5-enkephalin in aqueous solution is found to exist in both type II beta-turn and beta-sheet structures, whereas Met5-enkephalin has a lesser tendency to form beta-turn structure in aqueous solution. It is likely that these different conformers of enkephalins might bind to different receptor types.

Chemical Phenomena↗
PubMed1983

Synthesis of polypeptide models of elastin. Synthesis and properties of a cross-linked polytetrapeptide.

Synthesis of two copolymers, H-(phi-Pro-Gly-Gly)n-Val-OMe and H-(phi'-Pro-Gly-Gly)n-Val-OMe, where phi is Val or Lys and phi' is Val or Glu is described. Cross-linking between the two copolymers is achieved by a coupling reaction between the epsilon-amino groups of the lysine containing copolymer and delta-carboxyls of the glutamic acid of the other copolymer. The cross-linking reaction was performed during a temperature elicited phase separation with flow orientation of the copolymers. Coacervation of the intermediate polymers is presented, as is the scanning electron micrograph of the insoluble cross-linked product and its calcifiability as determined with electron probe microanalysis. The purity of the key intermediates and polymers is demonstrated by the usual analytical methods. Carbon-13 magnetic resonance spectra of the intermediate monomer units are included to validate the purity of their synthesis.

Cross-Linking Reagents↗
PubMed1982

Improved method for the analysis of furosemide in plasma by high-performance liquid chromatography.

Modifications of existing rapid high-performance liquid chromatographic procedures for the determination of furosemide in plasma were made in order to achieve greater sensitivity. To a small volume of plasma was added in internal standard structurally related to furosemide. Then, following previously described procedures, acetonitrile was added to precipitate the proteins and the clear supernatant was separated. However prior to injection of the supernatant the pH and composition of the sample were adjusted. This modification of the sample enabled an injection volume of up to 300 microliters of the supernatant to be injected onto the chromatographic column. The effluent was monitored spectrofluorimetrically. A standard linear calibration curve with a mean precision of +/- 4.4% was obtained for plasma samples containing 20--900 ng/ml of furosemide. Two structurally related compounds were used as internal standards in the furosemide assay.

Administration, Oral↗
PubMed1981

Reversed-phase high-performance liquid chromatographic analysis of liothyronine sodium and levothyroxine sodium in tablet formulations: preliminary studies on dissolution and content uniformity.

Levothyroxine sodium was estimated from tablet formulations of levothyroxine sodium and liotrix (liothyronine sodium-levothyroxine sodium combination tablet). The procedures consisted of the addition of 3,3-,5-triiodothyronine as the internal standard to the pulverized sample, followed by an acidic butanol extraction, evaporation, and injection onto a muBondapak reversed-phase high-performance liquid chromatographic column. The eluent was methanol-water-phosphoric acid (50:50:0.1), and the effluent was monitored by UV detection at 254 nm. A standard linear calibration curve was obtained for direct standard solutions equivalent to 18-225 micrograms of levothyroxine sodium/tablet. The procedure is sensitive enough for single-tablet analysis. Using this procedure, content uniformity studies were performed on liothyronine sodium tablets, levothyroxine sodium tablets, and liotrix tablets. The procedure also was adapted for conducting dissolution studies on levothyroxine sodium tablets in deionized water using the rotating-paddle method.

Chromatography, High Pressure Liquid↗
PubMed1980

Repeat polypeptide models of elastin as substrates for lysyl oxidase.

Synthetic repeat polypeptides analogous in sequence to the valine-rich regions of elastin have been tested as substrates for purified bovine aorta lysyl oxidase. These polypeptides, HCO(phi-Pro-Gly-Gly)n-Val-OMe, HCO(Val-Pro-Gly-phi-Gly)n-Val-OMe, and HCO-Val-(Ala-Pro-Gly-phi-Gly-Val)n-OMe, where phi = Val or Lys at approximately a 4:1 ratio and where n greater than or equal to 40, are models of the tetra-, penta-, or hexapeptide repeat sequences found in elastin. alpha-Aminoadipic delta-semialdehyde is generated in each of these upon incubation with lysyl oxidase at 37 degrees C, whereas the aldol and anhydrolysinonorleucine bifunctional cross-linkages were formed only in the incubation of enzyme with polypentapeptide. Incubation of the polypentapeptide at 55 degrees C, which enhances coacervation of the peptide, increases aldehyde formation and generates a much higher ratio of cross-linkages to aldehyde than occurred at 37 degrees C. These results demonstrate that lysyl oxidase can oxidize lysine in synthetic polypeptides and suggest important conformational aspects of lysyl oxidase substrates which may control substrate potential as well as the ability of peptidyl aldehyde, once formed by the enzyme, to condense to cross-linkage products.

Amino Acid Oxidoreductases↗
PubMed1978

Proton magnetic resonance and conformational energy calculations of repeat peptides of tropoelastin. A permutation of the hexapeptide.

The conformation of a hexapeptide sequence occurring in tropoelastin is discussed from the results obtained using a combined approach of theoretical conformational energy calculations on HCO-Val-Ala-Prb-Gly-OMe and 1h nmr studies on t-Boc-Val-Ala-Pro-Gly-Val-Gly-OMe in a dilute solution of methanol. Both studies have reasonable concurrence with respect to the preferred conformation of the hexapeptide and an analysis of the combined results suggests that the hexapeptide is stabilized by a beta-turn involving the Ala1,iC=O and Val4,iNH groups and a gamma-turn involving Gly5,iC=O and Gly3,iNH groups. A weaker interaction between Gly3,iC=O and Gly5,iNH groups is also found to be possible. Conformational features of the first valyl residue in the sequence Val-Ala-Pro-Gly-Val-Gly and the last valyl residue in Ala-Pro-Gly-Val-Gly-Val are compared and found to have similar torsion angles. The implications of such a similarity are discussed with respect to the conformation of the polyhexapeptide.

Amino Acid Sequence↗
PubMed1978

Coacervation properties in sequential polypeptide models of elastin. Synthesis of H-(Ala-Pro-Gly-Gly)n-Val-OMe and H-(Ala-Pro-Gly-Val-Gly)n-Val-OMe.

Syntheses of two sequential polypeptides H-(Ala-Pro-Gly-Gly)n-Val-OMe and H-(Ala-Pro-Gly-Val-Gly)n-Val-OMe via the p-nitrophenyl active ester procedure are reported. The two polymers were obtained in good yields and the polymers were shown to be of large molecular weights, n greater than 40. These two polypeptides were synthesized as analogs of the two coacervating sequential polypeptides H-(Val-Pro-Gly-Gly)n-Val-OMe, and H-(Val-Pro-Gly-Val-Gly)n-Val-OMe, in which the Val-l residue is replaced by an Ala-l residue. H-(Ala-Pro-Gly-Gly)n-Val-OMe did not coacervate even at as high a temperature as 100 degrees, and H-(Ala-Pro-Gly-Val-Gly)n-Val-OMe did not coacervate; however, it precipitated irreversibly around 65--70 degrees C. This suggests the critical role of the Val-Pro hydrophobic side chain interaction in coacervation.

Amino Acid Sequence↗