29 results match your criteria: "Kings College University of London[Affiliation]"
Biochem Soc Trans
November 1991
Biochemistry Section, School of Life, Basic Medical and Health Sciences, King's College University of London, U.K.
Matrix
July 1990
Biochemistry Department, Kings' College University of London, UK.
Elastin in vivo is likely to be complexed with amphipathic ligands such as lipids. The susceptibility of stable [3H] elastin-fatty acid complexes to the action of porcine pancreatic elastase (PPE) and to human neutrophil lysates over time was assessed. Elastolysis by PPE of substrates prepared with oleic or linoleic acids was initially higher (for up to 2 hours) than that of uncomplexed elastin.
View Article and Find Full Text PDFBiochem J
September 1987
Department of Biochemistry, King's College (University of London), U.K.
1. The intermediate structures formed during dialysis of mixtures of cholate, phospholipid and cytochrome c oxidase were analysed by gel chromatography and electron microscopy. Measurements of trapped phosphate and the degree of respiratory control were used to assess the integrity of the vesicular structures formed.
View Article and Find Full Text PDFJ Biomol Struct Dyn
December 1983
Department of Biophysics, King's College University of London, England.
The molecular structures of adducts between the + and - enantiomers of 7,8-diol 9,10-epoxy benzo[a]pyrene and a double-stranded model for DNA, have been examined by empirical energy calculations. Low-energy structures were only obtained for A form, and not B form DNA. Both + and - adducts are of approximately equal energy.
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