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Biomedical subjects

D Dahl

Publications and source records attributed to D Dahl.

At least 217 records · Page 12Linked to original sources
PubMed1978

Neurofilament protein in clonal lines of mouse neuroblastoma.

As indicated by immunofluorescence with neurofilament antiserum and by electron microscopy two neuroblastoma clones in suspension culture contained a pool of neurofilament subunits which could be induced to assemble into filaments following exposure to vinblastine and colchicine. Under the same culture conditions neuroblastoma cells treated with aluminum extended thick processes with many filaments. The processes were much smaller in nontreated cells but still contained bundles of filaments. These filaments persisted after inhibition of protein synthesis by cycloheximide. In the long neurites formed by cells attached to plastic immunofluorescence with neurofilament antiserum was particularly intense at the growth cone.

Aluminum↗
PubMed1977

Preparation of antisera to neurofilament protein from chicken brain and human sciatic nerve.

Antigens isolated by hydroxyapatite chromatography from human sciatic nerve (SN1 protein) and from 8 M urea extracts of chicken brain were selectively localized by immunofluorescence to neurofibrils in rat and chicken CNS. Absorption of the antisera with SN1 protein, chicken antigen or GFA protein abolished the staining. Antisera raised against antigen isolated with the same procedure from buffer extracts of chicken brain stained both neurofibrils and glial fibrils by immunofluorescence. Neurofibrillary staining was selectively abolished by absorption of the antisera with SN1 protein. Antisera prepared against axonal preparations isolated from bovine white matter only stained astroglia and were thus undistinguishable from anti-GFA sera in this respect. The data suggested that the protein subunits of neurofilament and glial filaments, although difficult to separate in brain extracts by standard biochemical procedures and by subcellular fractionation in bovine white matter, still retain immunological specificity. In addition, the immunological cross reactivity between human and chicken antigens suggested that neurofilaments, as other constituents of the cytoskeleton such as microtubules and actin microfilaments, show a high degree of evolutionary stability.

Animals↗
PubMed1977

[On the effect of hyperbaric oxygen (OHP) at the guinea pig's cochlea insulted by hypoxia (author's transl)].

The effect of OHP (oxygen under high pressure) by examining 17 CO-intoxicated guinea pigs. The following effects have been observed: The microphonics recovered significantly faster after hypoxia caused by CO than under air. Hyperbaric oxygen has a protecting effect on the inner ear. If OHP is applicated before CO, the microphonics decrease less than under normal breathing. The postmortal microphonics increased to a level above the known postmortal slope, suggesting a diffusion of oxygen through the round window.

Action Potentials↗
PubMed1977

[Determination of the perilymph density in the cochlea of guinea pigs (author's transl)].

The perilymph density of the sc. tympani, sc. vestibuli and the density of liquor cerebrospinalis in guinea-pigs are measured by determination from mass and volume of the fluid column in a glass capillary tube. For the density of perilymph in sc. vest. a value of (formula: see text) in sc. tymp. a value of (formula: see text), and for liquor a value of (formula: see text) was obtained.

Animals↗
PubMed1977

Specificity of the glial fibrillary acidic protein for astroglia.

Glial fibrillary acidic protein (GFA) is the main constituent of glial filaments and the close similarity of GFA and neurofilament protein has been recently reported. However, the immunofluorescence staining of peripheral nerve which may be observed with GFA antisera is not due to cross-reaction between GFA and neurofilament protein. Staining of peripheral axons was also observed with control sera obtained by injecting the rabbits with nonimmunogenic GFA preparations isolated with the same procedure. Immune GFA antisera and control sera reacted with sodium dodecyl sulfate extracts of sciatic nerve. However, the precipitin line formed with peripheral nerve crossed the line against GFA protein, thus indicating nonidentity between the two antigens. Buffer extract of sciatic nerves that had been incubated with spinal cord reacted by immunodiffusion with GFA antisera, thus indicating that redistribution of GFA occurred under these conditions.

Animals↗
PubMed1976

Isolation and initial characterization of glial fibrillary acidic protein from chicken, turtle, frog and fish central nervous systems.

The purification procedure for mammalian glial fibrillary acidic protein allowed the isolation of related proteins from the brain and spinal cord of the chicken, turtle, frog and fish. With the exception of the turtle, the proteins so isolated were homogeneous and migrated as a single band on sodium dodecyl sulfate-acrylamide gel electrophoresis, displaying the same mobility as bovine glial fibrillary acidic protein, 54 000 mol. wt. In the turtle an additional slower migrating band was constantly present, together with the main species. Mammalian and submammalian proteins were similar in amino acid composition and appeared to be susceptible to the same type of in situ proteolysis, with degradation of the major species into multiple polypeptides ranging down to 40 500 mol. wt. Unless degraded, the proteins isolated from submammalian vertebrates were excluded from sodium dodecyl sulfate-acrylamide gels if a reducing agent was not added to the electrophoretic sample, thus suggesting the existance of disulfide bridges between polypeptide chains, as demonstrated for the mammalian protein. The purified submammalian antigens cross-reacted with antisera to human glial fibrillary acidic protein with formation of spurs not only at the junction between mammalian and submammalian precipitation lines, but also between submammalian lines. The antisera produced against chicken antigen did not react with the human antigen and the antichicken sera could not be absorbed with human antigen. An immunologically active cyanogen bromide peptide in the myoglobin range (17 200 mol. wt.) characteristic of the mammalian protein, degraded and nondegraded, was not present in the digest of the submammalian proteins.

Amino Acids↗