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Biomedical subjects

J Fried

Publications and source records attributed to J Fried.

At least 109 records · Page 6Linked to original sources
PubMed1974

Carbon-13 relaxation and proton nuclear magnetic resonance studies of prostaglandin F2alpha.

Carbon magnetic resonance T(1) relaxation and chemical shift measurements at 22.63 MHz establish hydrophobic aggregation of prostaglandin F(2alpha) in phosphate buffer solutions between 0.05 and 0.2 M. Analysis of the proton magnetic resonance spectra of prostaglandin F(2alpha) at 270 MHz by double resonance techniques yield all the proton-proton coupling constants for the five-membered ring indicating a favored half-chair conformation for the ring in which the dihedral angle for the C-8 and C-12 protons is close to 180 degrees . Effective correlation times derived from carbon magnetic resonance T(1) values for all the carbon atoms show segmental motion for ring carbon C-10 and in the aliphatic portions of both side chains, while the double bonded portions of the side chains and the ring carbons act as a more rigidly interconnected network. Chemical shift changes in the carbon magnetic resonance and proton magnetic resonance spectra upon aggregation suggest that the 5-6 double bond, C-7, and C-9 participate in the aggregation process.

Carbon Isotopes↗
PubMed1973

Carbon-13 nuclear magnetic resonance spectra of prostaglandins and some prostaglandin analogs.

High-resolution pulsed Fourier-transform nuclear magnetic resonance spectroscopy at 22.63 MHz was used to observe the proton-decoupled natural-abundance (13)C nuclear magnetic resonance spectra of CDCl(3) solutions of the methyl esters of prostaglandins F(1alpha), 15-epi-F(1alpha), F(2alpha), F(2beta), E(2), A(2), 13-dehydro-F(2alpha), 13-dehydro-F(3alpha), two intermediates on the synthetic pathway to 13-dehydro-PGF(3alpha), and of 7-oxa-PGF(1alpha). All resonances were assigned by chemical shift comparisons and single-frequency offresonance proton decoupling. With two exceptions, all the lines of the spectra are well-resolved single-carbon resonances. Those due to the cyclopentane and vinyl carbons are most sensitive to structural changes. Some of these effects can be rationalized in terms of the preferred conformations of the molecules.

Carbon Isotopes↗
PubMed1972

Morphine-3-succinyl--bovine serum albumin: an immunogenic hapten-protein conjugate.

Morphine-3-hemisuccinate was synthesized by reaction of morphine with succinic anhydride. This compound was conjugated to bovine serum albumin by the mixed anhydride method, and the degree of conjugation was determined by base hydrolysis of the conjugate, extraction, and measurement of free morphine. An average of 6.5 molecules of morphine were conjugated to each molecule of protein. Eleven rabbits immunized with varying doses of the conjugate were producing antibody 8 weeks later, as determined by a modification of the ammonium sulfate method, which measures primary binding of antigen by antibody.

Animals↗