Antibody responses in cell cultures from draining and non-draining rabbit lymph nodes primed with native or polymerized human albumin.
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Animals↗
Biomedical subjects
C H Self
Publications and source records attributed to C H Self.
The isocitrate dehydrogenases of Acinetobacter lwoffi. Studies on the regulation of a nicotinamide-adenine dinucleotide phosphate-linked isoenzyme.
Of the two NADP-linked isocitrate dehydrogenases in Acinetobacter lwoffi the higher-molecular-weight form, isoenzyme-II, is reversibly stimulated sixfold by low concentrations of glyoxylate or pyruvate. Kinetic results indicate that this stimulation of activity involves both an increase in V(max.) and a decrease in the apparent K(m) values for substrates, most markedly that for NADP(+). Other changes brought about by glyoxylate or pyruvate include a shift in the pH optimum for activity and an increased stability to inactivation by heat or urea. Mixtures of glyoxylate plus oxaloacetate, known to inhibit isocitrate dehydrogenases from other organisms, produce inhibition of both A. lowffi isoenzymes, and do not reflect the stimulatory specificity of glyoxylate for isoenzyme-II. Isoenzyme-II is also stimulated by AMP and ADP, but the activation by glyoxylate or pyruvate is shown to be quite independent of the adenylate activation. Differential desensitization of the enzyme by urea to the two types of activator further supports the view that the enzyme possesses two distinct allosteric regulatory sites. The metabolic significance of the activations is discussed.
Adenosine Diphosphate↗
The spontaneous induction of anamnestic antibody synthesis in lymph node cell cultures many months after primary immunization.
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Animals↗
The isocitrate dehydrogenases of Acinetobacter lwoffi. Separation and properties of two nicotinamide-adenine dinucleotide phosphate-linked isoenzymes.
Two isoenzymes of NADP-linked isocitrate dehydrogenase have been identified in Acinetobacter lwoffi and have been termed isoenzyme-I and isoenzyme-II. The isoenzymes may be separated by ion-exchange chromatography on DEAE-cellulose, by gel filtration on Sephadex G-200, or by zonal ultracentrifugation in a sucrose gradient. Low concentrations of glyoxylate or pyruvate effect considerable stimulation of the activity of isoenzyme-II. The isoenzymes also differ in pH-dependence of activity, kinetic parameters, stability to heat or urea and molecular size. Whereas isoenzyme-I resembles the NADP-linked isocitrate dehydrogenases from other organisms in having a molecular weight under 100000, isoenzyme-II is a much larger enzyme (molecular weight around 300000) resembling the NAD-linked isocitrate dehydrogenases of higher organisms.
Alcaligenes↗
In vitro regulation of the anamnesic antibody response upon addition of heterologous antigens to primed lymphoid cells.
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Animals↗
Separation of isoenzymes by zonal centrifugation.
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Alcaligenes↗
A new sensitive and fast peptide immunoassay based on enzyme amplification used in the determination of CGRP and the demonstration of its presence in the thyroid.
An enzyme amplified immunoassay for rCGRP based on cofactor cycling has been found to be clearly superior to a comparable radioimmunoassay employing the same antiserum in terms of sensitivity, speed and convenience. Correlation between the two methods was very good. With the enzyme amplified immunoassay we have been able to demonstrate the existence of rCGRP in thyroid extract.
Animals↗