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Biomedical subjects

G R Stibitz

Publications and source records attributed to G R Stibitz.

17 recordsLinked to original sources
PubMed1987

A computer method for the acquisition and analysis of patch-clamp single-channel currents.

The method we present instructs the computer to deliver sets of programmed membrane voltages and allows the acquisition of large amounts of digitized data, compact storage, ready identification of records and rapid, interactive analysis of channel current data. A typical cycle of analysis including amplitude determination and kinetic measurements for 10 s of continuous data digitized at 5 kHz requires 5-20 min depending on the complexity of the observed channel activity. This procedure is compatible with such storage protocols as that described by Bezanilla [Biophys. J., 47 (1985) 437-441], although there are obvious benefits to using standard computer storage devices such as hard disks, floppy disks, and Bernoulli Boxes. The programs described in this report are available from the authors.

Animals↗
PubMed1974

Studies of impedance in cardiac tissue using sucrose gap and computer techniques. II. Circuit simulation of passive electrical properties and cell-to-cell transmission.

The impedance measured in a strip of heart tissue from the moth Hyalophora cecropia is fitted by circuit models of several configurations. The circuits include: (a) a single R-C circuit (b) a double R-C circuit (c) terminated transmission lines, and (d) a pattern of cells with cell-to-cell transmission paths. The last of these is found to give the best fit. Calculation of the model impedances and optimization of element values are performed by a computer. The possibility that the mechanism of cell-to-cell transmission may be capacitative rather than conductive is explored using values of capacitance derived from the circuit models to calculate the effect of capacitative coupling alone on signal transmission. The calculations show that sufficient voltage can be transmitted from the excited cell to an adjacent cell to effect excitation.

Animals↗
PubMed1973

Studies of impedance in cardiac tissue using sucrose gap and computer techniques. I. The influence of sucrose and oil as insulating media.

Impedances of cardiac cells of an insect were determined as a function of time to test the effects of sucrose and oil as insulating media in a gap arrangement. Impedance values are shown to increase markedly with time when sucrose is used as the insulating agent. Although impedance values are steady when oil is used, it is suggested that a layer of trapped electrolyte provides a shunt pathway and seriously impairs the validity of the measurements. A quick wash with sucrose followed by oil does not alleviate the situation but leaves a layer of sucrose trapped at the tissue-medium interface into which ions diffuse. The hypotheses (a) that the diffusion of intracellular K(+) into the sucrose would result in an increase in tissue impedance and (b) that a layer of trapped electrolyte under the oil film provides a shunt pathway are examined by computer analyses of a simple model.

Animals↗
PubMedDate not supplied

Binding of iophenoxate and iopanoate to human serum albumin.

Determination of the binding affinities of 125I-labeled cholecystographic agents to human serum albumin by ultrafiltration techniques is complicated by the appearance of radiochemical impurities resulting from radiolysis of the parent compound. With labeled compounds purified daily by two extractions through chloroform, iophenoxic acid has an extremely high binding affinity. The dissociation constant (K) is 0.013 micronM for iophenoxate, compared to 0.15 micronM for iopanoate, its close analogue. However, at the weaker sites, iophenoxic acid is less strongly bound than iopanoate. The exceptionally high affinity of iophenoxate for a single site of serum albumin appears to underlie its unusual persistence in plasma. Binding in vivo is reversible and not covalent in nature. The choleretic compounds cinchophen and taurocholate have differential effects on the biliary excretion of iophenoxate and iopanoate. This cannot be attributed to selective inhibition of binding to plasma protein.

Crystallization↗
PubMedDate not supplied

Competition for binding to multiple sites of human serum albumin for cholecystographic agents and sulfobromophthalein.

The binding of two cholecystographic agents, iophenoxate and iopanoate, to human serum albumin was studied with 11 putative competitors; the results were qualitatively consistent with competitive binding to common sites. A more precise analysis of competition was achieved with four pairs of compounds for which the free and bound concentration of each was determined. The results were analyzed by a computer program and the dissociation constants calculated for both binder and competitor at specified sites on albumin. With numbering based on the rank order of dissociation constants for iophenoxate, the highest binding of the four compounds occurs at different sites: iophenoxate at site I; iopanoate at site II, sulfobromophthalein at site III; and bromphenol blue at site II. For a given compound, there is close agreement in the calculated affinities at different sites regardless of the competitor.

Binding Sites↗