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F Lederer

Publications and source records attributed to F Lederer.

162 records · Page 9Linked to original sources
PubMed1974

Homology between bakers' yeast cytochrome b2 and liver microsomal cytochrome b5.

The amino-acid sequence of the hemebinding region of bakers' yeast cytochrome b(2) [L-(+)-lactate dehydrogenase, EC 1.1.2.3] has been determined. It shows a strong similarity with the sequence of microsomal cytochrome b(5), and appears to be compatible with the same kind of peptide-chain folding, in agreement with data obtained previously by various physiochemical methods. The comparison shows that the fifth and sixth heme ligands must be histidine residues, thus substantiating previous conclusions drawn in particular from photooxidation experiments and nuclear magnetic resonance studies. The data reported in this paper suggest a common origin for the two proteins. Implications for their biochemical evolution are presented.

Amino Acid Sequence↗
PubMed1971

Présence de la epsilonN-trimethyllysine dans l'iso-1 et l'iso-2 cytochromes c synthétisés par des souches de levure à déficience respiratoire (varrho(-)).

It is shown that the iso-1 and iso-2 cytochromes c synthesized by two strains of respiratory deficient strains of yeast (varrho(-)) possess one residue of epsilonN-trimethyllysine and do not differ in this respect from the iso-cytochromes produced by varrho(+) strains. This result excludes the possibility that the methylation reaction is linked to respiratory activity or to the varrho(+) factor.

Journal Article↗
PubMedDate not supplied

Perfluoroalkylphosphocholines are poor protein-solubilizing surfactants, as tested with neutrophil plasma membranes.

We have tested the membrane-protein solubilizing properties of two perfluoroalkylphosphocholines. These compounds belong to a series of fluorinated amphiphiles which are being investigated as potential stabilizing agents for a variety of fluorocarbon-based systems. We are particularly interested in cytochrome b558 from phagocytes, the redox component of NADPH oxidase. Its heavy subunit is believed to carry binding sites for NADPH and FAD. Nevertheless, when the cytochrome is purified in the presence of classical detergents, it carries no FAD. This could be due to a delipidating, denaturing effect of these detergents (octyl glucoside, Triton, etc). The first perfluoroalkyphosphocholine, C8F17(CH2)2O-P(O2-)-O(CH2)2N+(CH3)3(F8C2PC), extracted about as much protein from neutrophil plasma membranes into a 100,000 g supernatant as octyl glucoside. The second compound, C8F17(CH2)11O-P(O2-)-O(CH2)2N+(CH3)3(F8C11PC), was less efficient. We found that flavin was still protein-bound in the crude F8C2PC extract at a FAD to heme ratio of about 1, and a good NADPH oxidase activity was obtained without addition of exogenous FAD, even after dialysis or gel filtration, whereas dialysis eliminated most of the FAD from the octyl glucoside extracts. These experiments appeared to make F8C2PC an interesting membrane-solubilizing agent. Nevertheless, no protein in the F8C2PC extract could be adsorbed on the chromatographic supports normally used for purification. After dilution of the extract and addition of 15 mM octyl glucoside, some of the proteins, such as myeloperoxidase, could be adsorbed (and eluted), but not cytochrome b558. Freeze-fracture electron microscopy showed that the F8C2PC extracts contained numerous vesicles and aggregates of small shapeless particles. Higher centrifugal forces sedimented most proteins of the 100,000 g supernatant. As a check, the effect of F8C2PC was tested on sarcoplasmic reticulum vesicles, the behavior of which with respect to the usual non-denaturating detergents has been well studied. There was little, if any, solubilization. We conclude that, although supernatants of F8C2PC extracts of neutrophil membranes are optically clear, proteins are not really solubilized. This result is in keeping with the absence of lytic effects of F8C2PC on erythrocyte membranes.

Cell Membrane↗