PubMed Health⌕ Search

Biomedical subjects

F L Crane

Publications and source records attributed to F L Crane.

At least 19 recordsLinked to original sources
PubMed1979

Distribution of insulin receptors among mouse liver endomembranes.

Specific binding of insulin to highly purified preparations of rough endoplasmic reticulum, Golgi apparatus, and plasma membrane of mouse liver was determined. 125I-labeled insulin bound maximally to the plasma membrane in radio-receptor assays. Golgi apparatus fractions exhibited binding 10--20% that of plasma membrane and rough endoplasmic reticulum exhibited only 1--2% of plasma membrane binding. Binding was proportional to membrane concentration and dose vs. response curves were very similar for the different fractions. Scatchard analysis of the insulin binding data for the plasma membrane and Golgi apparatus fractions showed curvilinear plots yielding similar apparent binding affinities (0.9 and 3.0-10(8) M-1, respectively). Purity of the isolated endomembranes was analyzed by morphometry and (Na+ + K+ + Mg2+)-ATPase and these preparations displayed less than 1% contamination by plasma membrane. These findings provide important confirmation of the presence of insulin receptors in Golgi apparatus membranes comparable to those located on the plasma membrane. Finally, the present study did not allow us to verify the existence of insulin receptors in the endoplasmic reticulum.

Animals↗
PubMed1979

Catechols stimulate ferricyanide reduction in chloroplast photosystem II.

In isolated chloroplasts (Spinacia olearacea), where electron transport to Photosystem I is blocked by the plastoquinone antagonist, dibromothymoquinone, lipophilic catechols in concentrations of 50--150 microM stimulate ferricyanide reduction in Photosystem II and associated O2 evolution. Non-permeating catechols, such as Tiron, are unable to stimulate this reaction. Those quinones, such as 2,5-dimethylbenzoquinone, which act as class III electron acceptors, do not lead to stimulation of ferricyanide reduction in Photosystem II or stimulation fo associatied O2 evolution, when electron transport to Photosystem I is blocked by dibromoquinone. Stimulation of ferricyanide reduction is not observed in Tris-treated chloroplasts, implying that electron donation to Photosystem II by catechols is not responsible for the stimulation. Various mechanisms for this stimulation in class II chloroplasts are discussed.

Catechols↗
PubMed1978

Cytochemical demonstration of glutaraldehyde-resistant NADH-ferricyanide oxido-reductase activities in rat-liver plasma membranes and Golgi apparatus.

NADH-ferricyanide reductase activity was demonstrated in rat liver endomembranes by cytochemical procedures. The activity observed in plasma membrane and mature portions of the Golgi apparatus resisted fixation in 0.1% glutaraldehyde, a characteristic which permitted differentiation of the NADH-ferricyanide reductase of plasma membranes and mature Golgi apparatus elements from those of mitochondria, microbodies, endoplasmic reticulum and nuclear envelope. With the latter membranes, activity could be demonstrated only with unfixed material or following brief glutaraldehyde fixation and was greatest with broken cells or isolated fractions due to problems of penetration of reagents. Biochemical studies paralleled cytochemical findings with respect to glutaraldehyde fixation and sensitivity to other metabolic inhibitors. The findings provide evidence that a NADH-ferricyanide reductase may be among the membrane constituents conserved and/or modified during flow differentiation of membranes. The basis for a method to evaluate plasma membrane contamination of endoplasmic reticulum fractions and to differentiate among mature and immature secretory vesicles of the Golgi apparatus is also indicated.

Animals↗
PubMed1977

Different effects of inhibitors on two mutants of Escherichia coli K12 affected in the Fo portion of the adenosine triphosphatase complex.

The effects of the inhibitors dicyclohexyl-carbodiimide (DCCD), bathophenanthroline and tertiary octylcatechol, on some enzyme activities in membranes from strains of Escherichia coli carrying mutations in the uncB or uncC genes have been studied. Membranes prepared from uncC mutants retain a normal DCCD-sensitive Mg2+-stimulated adenosine triphosphatase (Mg-ATPase) activity whereas in uncB mutants this enzyme activity is insensitive to DCCD. The membrane-bound Mg-ATPase activity from the uncC mutant strain, as compared with that from the normal strain, is only partially sensitive to the inhibitors bathophenanthroline or tertiary-octylcatechol. Both of these inhibitors stimulate the membrane-bound Mg-ATPase from uncB mutant strains. A DCCD-insensitive Mg-ATPase activity is found in the cytoplasmic fraction following cell disruption of either the uncB or the uncC mutants. The lipophilic chelators bathophenanthroline and tertiary-octylcatechol stimulate the activity of the 'soluble' Mg-ATPase in the uncB mutant but partially inhibit the activity in the uncC mutant. The NADH oxidase activities in membranes from both mutant and normal strains are strongly inhibited by tertiary-octylcatechol and bathophenanthroline but not by DCCD.

Adenosine Triphosphatases↗
PubMed1976

Inhibition of mitochondrial electron transport by hydrophilic metal chelators. Determination of dehydrogenase topography.

The topography of the inner mitochondrial membrane was investigated using inhibitors of electron transport on preparations of beef heart mitochondria and electron transport particles of opposite orientation. Reductions of juglone, ferricyanide, indophenol, coenzyme Q, duroquinone, and cytochrome c by NADH are inhibited to different extents on both sides of the membrane by the impermeant hydrophilic chelators bathophenanthroline sulfonate and orthophenanthroline. The extent of inhibition for each acceptor increased in the order given. At least two chelator-sensitive sites are present on each membrane face between the flavoprotein and coenzyme Q and a chelator-sensitive site is present on the matrix face between the sites of coenzyme Q and duroquinone interaction. Duroquinol oxidation in mitochondria only is stimulated by bathophenanthroline sulfonate. Juglone reduction is stimulated in electron transport particles (only) by p-hydroxymercuribenzenesulfonate, but after mercurial treatment, juglone reduction in both particles and mitochondria is more sensitive to bathophenanthroline sulfonate. Succinate dehydrogenase components are inhibited by hydrophilic orthophenanthroline or bathophenanthroline sulfonate in mitochondria only. Electron flow between the dehydrogenases of succinate and NADH occurs via a chelator-sensitive site located on the matrix face of the membrane. Inter-complex electron flow is prevented by rotenone or thenoyltrifluoroacetone. The lack of succinate-indophenol reductase inhibition by bathophenanthroline sulfonate in the presence of rotenone or thenoyltrifluoroacetone indicates that the rotenone-sensitive site may be located on the matrix face and demonstrates that electrons flow between the NADH and succinate dehydrogenases via a hydrophilic chelator and rotenone-thenoyltrifluoroacetone-sensitive site on the matrix face of the membrane. Inhibiton by hydrophilic chelators only in mitochondria indicates that succinate dehydrogenase as well as NADH dehydrogenase has a transmembranous orientation.

Animals↗