Published in Biochimica et Biophysica Acta
This study is an investigation of the ability of the bacterial channel alpha-hemolysin to facilitate water permeation across biological membranes. alpha-Hemolysin channels were incorporated into rabbit erythrocyte ghosts at varying concentrations, and water permeation was induced by mixing the ghosts with hypertonic sucrose solutions. The resulting...
Published in Biochimica et Biophysica Acta
Published in Biochimica et Biophysica Acta
(1) Nagarse, a bacterial protease, was permitted to react with sarcoplasmic reticulum, submitochondrial and plasma membranes. Gel electrophoresis indicated that all polypeptides were labile to the enzyme, and therefore must be at least partially exposed at membrane surfaces. However, hydrolysis did not proceed to completion, and in each membrane 30...
Published in Biochimica et Biophysica Acta
Published in Biochimica et Biophysica Acta
Past work has shown that general anesthetics perturb the membranes of isolated synaptic vesicles, thereby increasing permeability to protons and inhibiting the ability of the vesicles to take up catecholamines. It has been proposed that such effects may produce anesthesia through inhibition of synaptic transmission. The mechanisms of perturbation i...
Published in Biochimica et Biophysica Acta
Published in Biochimica et Biophysica Acta
Published in Biochimica et Biophysica Acta
Published in Biochimica et Biophysica Acta
We tested the ability of saturated n-monocarboxylic acids ranging from eight to 12 carbons in length to self-assemble into vesicles, and determined the minimal concentrations and chain lengths necessary to form stable bilayer membranes. Under defined conditions of pH and concentrations exceeding 150 mM, an unbranched monocarboxylic acid as short as...
Published in Biochimica et Biophysica Acta
We are investigating the properties of pre-existing membrane structures that may contribute to localization of newly formed polypeptides on target membranes. To this end, D-beta-hydroxybutyrate dehydrogenase (EC 1.1.1.30) was purified from inner membranes of rat liver mitochondria and interacted with three different cellular membranes, as well as w...
