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Biomedical subjects

J A Hamilton

Publications and source records attributed to J A Hamilton.

At least 343 records · Page 19Linked to original sources
PubMed1973

Induction of a primary antihapten response in vivo by a graft-vs.-host reaction.

A primary anti-NIP PFC response can be elicited by a GVH reaction provided certain structural requirements of the NIP-carrier are met. NIP-coated F(1) erythrocytes and NIP-coated parental erythrocytes give rise to substantial anti-NIP PFC responses in F(1) mice after the injection of parental spleens. These conjugates do not of themselves give rise to an anti-NIP PFC response and, in fact, normally give rise to NIP-specific tolerance. In contrast the GVH reaction is not able to enhance the primary anti-NIP PFC response to immunogenic NIP-conjugates.

Animals↗
PubMed1973

Natural abundance carbon-13 nuclear magnetic resonance spectra of the canine sciatic nerve.

The proton-decoupled natural abundance carbon-13 nuclear magnetic resonance spectrum of the canine sciatic nerve is virtually identical to that of canine adipose tissue and markedly similar to that of liquid triolein. No resonances assignable to cholesterol, glycolipids, or sphingolipids are detectable in the sciatic nerve spectrum despite their abundance in the myelin sheath of this nerve. However, many such resonances are observed in lipid extracts of the nerve. Chronmatographic analysis of specimens of canine and rabbit sciatic nerve has revealed that these contain sufficient triglyceride to account quantitatively for the observed spectrum. Proton nuclear magnetic resonance and spin-labeling results for preparations containing myelin, especially those derived from the peripheral nerve, should be critically examined for experimental artifacts reflecting the triglyceride content.

Adipose Tissue↗
PubMed1973

Natural abundance carbon-13 nuclear magnetic resonance spectra of human serum lipoproteins.

Human serum lipoproteins have been studied by Fourier transform nuclear magnetic resonance of carbon-13 in natural abundance. Spectra of highdensity, low-density, and very-low-density lipoproteins were recorded and partly assigned. The prominent features of these spectra reflect the qualitative and quantitative composition of the lipid moiety of these complexes. The results suggest that carbon-13 nuclear magnetic resonance will be a useful technique for studies of the structural and dynamic parameters of lipoproteins.

Carbon Isotopes↗
PubMed1972

Biochemical and genetic studies on ubiquinone biosynthesis in Escherichia coli K-12:4-hydroxybenzoate octaprenyltransferase.

Three ubiquinone-deficient mutants of Escherichia coli unable to convert 4-hydroxybenzoate into 3-octaprenyl-4-hydroxybenzoate were isolated and examined. The results of genetic analysis suggest that each of the mutants carries a mutation in a gene designated ubiA which can be represented at minute 79 on the E. coli chromosome map. The conversion of 4-hydroxybenzoate into 3-octaprenyl-4-hydroxybenzoate, catalyzed by 4-hydroxybenzoate octaprenyltransferase, was studied with a strain of E. coli that is blocked in the common pathway of aromatic biosynthesis and consequently accumulates the precursor of the side chain of ubiquinone. Both the side-chain precursor and 4-hydroxybenzoate octaprenyltransferase were shown to be membrane-bound. The enzyme required Mg(2+) for optimal activity. The ubiA(-) mutants were found to lack 4-hydroxybenozate octaprenyltransferase activity, which suggested that the ubiA gene is the structural gene coding for this enzyme.

Alkyl and Aryl Transferases↗
PubMed1971

Ubiquinone biosynthesis in Escherichia coli K-12. Accumulation of an octaprenol, farnesylfarnesylgeraniol, by a multiple aromatic auxotroph.

Cell extracts of a multiple aromatic auxotroph of Escherichia coli K-12, strain AB2830, grown in the absence of precursors of the quinone rings of the ubiquinone and menaquinone molecules, converted 4-hydroxy[U-(14)C]benzoate into a mixture of 3-octaprenyl-4-hydroxybenzoate and 2-octaprenylphenol. An octaprenol, farnesylfarnesylgeraniol, was isolated from such cell extracts and characterized by n.m.r. and mass spectroscopy. Neither the octaprenol, nor polyprenylation of 4-hydroxy[U-(14)C]benzoate, could be detected in cell extracts of strain AB2830 grown in the presence of 0.1mm-4-hydroxybenzoate. It was concluded that, in the biosynthesis of ubiquinone, the polyprenyl side chain is added to 4-hydroxybenzoate as a C(40) unit, the active form of which is converted by cell extracts into farnesylfarnesylgeraniol. The multiple aromatic auxotroph, when grown in the absence of 4-hydroxybenzoate but in the presence of 4-aminobenzoate, converted the latter compound into 3-octaprenyl-4-aminobenzoate. This compound was isolated from whole cells and characterized by n.m.r. and mass spectroscopy.

Alcohols↗
PubMed1970

The function of ubiquinone in Escherichia coli.

1. The function of ubiquinone in Escherichia coli was studied by using whole cells and membrane preparations of normal E. coli and of a mutant lacking ubiquinone. 2. The mutant lacking ubiquinone, strain AN59 (Ubi(-)), when grown under aerobic conditions, gave an anaerobic type of growth yield and produced large quantities of lactic acid, indicating that ubiquinone plays a vital role in electron transport. 3. NADH and lactate oxidase activities in membranes from strain AN59 (Ubi(-)) were greatly impaired and activity was restored by the addition of ubiquinone (Q-1). 4. Comparison of the percentage reduction of flavin, cytochrome b(1) and cytochrome a(2) in the aerobic steady state in membranes from the normal strain (AN62) and strain AN59 (Ubi(-)) and the effect of respiratory inhibitors on these percentages in membranes from strain AN62 suggest that ubiquinone functions at more than one site in the electron-transport chain. 5. Membranes from strain AN62, in the absence of substrate, showed an electron-spin-resonance signal attributed to ubisemiquinone. The amount of reduced ubiquinone (50%) found after rapid solvent extraction is consistent with the existence of ubiquinone in membranes as a stabilized ubisemiquinone. 6. The effects of piericidin A on membranes from strain AN62 suggest that this inhibitor acts at the ubiquinone sites: thus inhibition of electron transport is reversed by ubiquinone (Q-1); the aerobic steady-state oxidation-reduction levels of flavins and cytochrome b(1) in the presence of the inhibitor are raised to values approximating those found in the membranes of strain AN59 (Ubi(-)); the inhibitor rapidly eliminates the electron-spin-resonance signal attributed to ubisemiquinone and allows slow oxidation of endogenous ubiquinol in the absence of substrate and prevents reduction of ubiquinone in the presence of substrate. It is concluded that piericidin A separates ubiquinone from the remainder of the electron-transport chain. 7. A scheme is proposed in which ubisemiquinone, complexed to an electron carrier, functions in at least two positions in the electron-transport sequence.

Amobarbital↗