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Biomedical subjects

G C Roberts

Publications and source records attributed to G C Roberts.

At least 199 records · Page 11Linked to original sources
PubMed1975

A nuclear magnetic resonance study of nicotinamide adenine dinucleotide phosphate binding to Lactobacillus casei dihydrofolate reductase.

The binding of NADP+ to dihydrofolate reductase (EC 1.5.1.3) in the presence and absence of substrate analogs has been studied using 1H and 13C nuclear magnetic resonance (NMR). NADP+ binds strongly to the enzyme alone and in the presence of folate, aminopterin, and methotrexate with a stoichiometry of 1 mol of NADP+/mol of enzyme. In the 13C spectra of the binary and ternary complexes, separate signals were observed for the carboxamide carbon of free and bound [13CO]NADP+ (enriched 90% in 13C). The 13C signal of the NADP+-reductase complex is much broader than that in the ternary complex with methotrexate because of exchange line broadening on the binary complex signal. From the difference in line widths (17.5 +/- 3.0 Hz) an estimate of the dissociation rate constant of the binary complex has been obtained (55 +/- 10 sec-1). The dissociation rate of the NADP+-reductase complex is not the rate-limiting step in the overall reaction. In the various complexes studied large 13C chemical shifts were measured for bound [13CO]NADP+ relative to free NADP+ (upfield shifts of 1.6-4.3 ppm). The most likely origin of the bound shifts lies in the effects on the shieldings of electric fields from nearby charged groups. For the NADP+-reductase-folate system two 13C signals from bound NADP+ are observed indicating the presence of more than one form of the ternary complex. The IH spectra of the binary and ternary complexes confirm both the stoichiometry and the value of the dissociation rate constant obtained from the 13C experiments. Substantial changes in the IH spectrum of the protein were observed in the different complexes and these are distinct from those seen in the presence of NADPH.

Amides↗
PubMed1975

The kinetics of the interaction of heterologous anti-tumor serum and heterologous complement in non-tumor bearing mice.

The persistence of heterologous antitumor serum in the periphery of normal, non-tumor bearing mice was analyzed following intravenous, intraperitoneal, and subcutaneous injection. Intravenous injection of guinea pig complement subsequent to antibody administration resulted in the immediate disappearance of tumor-specific antibody from the periphery. Such studies suggest that appropriate therapy by the passive administration of antiserum requires the initial administration of antibody to allow for preferential binding to tumor-specific antigens followed by the subsequent injection of complement to mediate tumor cytolysis.

Animals↗
PubMed1973

Direct measurement of the pK values of an alkaline Bohr group in human hemoglobin.

Proton nuclear magnetic resonance spectra of normal and des-(his 146beta) human hemoglobin in the aromatic resonance region have been compared at different pH values. From these measurements, a pK value for histidine 146beta of 7.1 in carbonmonoxyhemoglobin and 8.0 in deoxyhemoglobin has been found. These pK values confirm the proposed role of histidine 146beta in the alkaline Bohr effect.

Carboxyhemoglobin↗