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Biomedical subjects

B Hess

Publications and source records attributed to B Hess.

At least 181 records · Page 10Linked to original sources
PubMed1979

Circular dichroic evidence for a conformational change in a cytochrome b--c1 complex by uncoupling agents.

Circular dichroic spectra of the cytochrome b--c1 complex exhibit bilobe formation typical of exciton splitting in the presence of uncoupler. Bilobe formation occurs if both cytochrome c1 and cytochrome b are fully reduced. The fully oxidized and ascorbate-reduced complexes are not altered dichroically by uncouplers. The exciton splitting induced by uncoupler is consistent with heme--heme interaction: specifically, interaction between the two cytochromes b in the complex.

Circular Dichroism↗
PubMed1979

The glycolytic oscillator.

The glycolytic oscillator, mainly studied in yeast, is described with respect to its overall dynamic and biochemical properties and the kinetics of its master enzyme phosphofructokinase. Biochemical and kinetic analyses are complemented by analysis of mathematical models. In addition to the discussion of structure and function of the glycolytic oscillator under homogeneous spatial conditions, recent theoretical and biochemical experiments demonstrating spatial pattern formation are also discussed, followed by a presentation of physiological viewpoints.

Adenine Nucleotides↗
PubMed1978

Circular-dichroism studies of the cytochrome b-c1 complex of Saccharomyces cerevisiae.

1. Circular dichroism studies on the Soret region of the cytochrome b-c1 complex of yeast reveal a change in the dichroism of cytochrome c1 depending on the redox state of cytochrome b, indicating a conformational interaction between both cytochromes. 2. This interaction is not influenced by binding of the inhibitor antimycin A to the complex, so that the interaction does not appear to be involved in the mechanism of electron transport through the complex. 3. Antimycin A binding causes a complex set of changes in the CD spectrum of the complex, which can be attributed to a severe and specific distortion of the environment of the chromophore of cytochrome b.

Antimycin A↗
PubMed1978

Photoselection and aggregation in purple membrane of Halobacterium halobium.

Preparations of the purple membrane of Halobacterium halobium suspended in dilute buffer and basal salt have been examined by circular dichroism spectroscopy and correlation analysis of scattered laser light. Dark adapted samples suspended in basal salt show photoselection when examined by circular dichroism. This was confirmed by irradiation with plane polarized light. Light-adapted samples or dark-adapted samples suspended in dilute buffer did not show this phenomenon. The reaction responsible for photoselection was shown to be the light induced cis-trans isomerization of bacteriorhodopsin. The stability of the induced anisotropy was due to aggregation in the basal salt suspensions which occurred despite little or no visual indication. This aggregation was confirmed by correlation analysis of scattered laser light.

Bacteriorhodopsins↗
PubMed1978

Binding and degradation of human 125I-HDL by rat adrenocortical cells.

In order to learn more about the mechanism by which high density lipoprotein (HDL) cholesterol is taken up by the adrenal cortex, binding and degradation of human 125I-HDL by suspensions of intact rat adrenal cortical cells have been examined. Cellular accumulation of 125I-HDL was found to occur in two phases. Our results indicate that the initial phase of association results from reversible binding of 125I-HDL to a specific saturable set of membrane binding sites. Binding site affinity appears equal for both rat and human HDL while affinity for human LDL is approximately one order of magnitude less on the basis of apoprotein weight. In addition, isolated rat adrenal cortical cells were found to degrade human 125I-HDL at a rapid rate. Degradation, like binding, can be prevented by addition of excess unlabeled HDL suggesting that binding and degradation are linked. Thus, one mechanism that could account for adrenal uptake of HDL cholesterol is endocytosis, initiated by lipoprotein binding to the HDL specific membrane binding site.

Adrenal Cortex↗