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Biomedical subjects

A Elgsaeter

Publications and source records attributed to A Elgsaeter.

8 recordsLinked to original sources
PubMed1978

Animal carotenoids 15. Carotenoid distribution and carotenoprotein of Asterias rubens.

A clear differentiation in localization according to functional groups in the carotenoids of the starfish, Asterias rubens, is reported. Only the free alpha-ketols, 7,8,7',8'-tetradehydroastaxanthin, 7,8-didehydroastaxanthin and astaxanthin, are present in the purified carotenoprotein. A post mortem liberated slime contained beta,beta-carotene, free and esterified alloxanthin and esterified alpha-ketols. Evidence suggesting the existence of an alloxanthin protein complex was obtained. The carotenoprotein, asteriarubin, accounts for approx. 10% of the protein extracted by low salt dialysis from the purple-blue part of the top skin of A. rubens and exhibits an absorbance maximum at 554 nm in buffer solution. Asteriarubin is a glycoprotein with an equivalent Stoke's radius corresponding to that of globular proteins of molecular weight 8--10 10(4) and contains 20 microgram carotenoid per mg asteriarubin. Sodium dodecyl sulfate polyacrylamide gel electrophoresis of purified asteriarubin disclosed two major components, one of which is a glycopeptide.

Animals↗
PubMed1978

Human spectrin. I. A classical light scattering study.

Human spectrin heterodimers were analyzed in solutions containing different amounts of salt employing the classical light scattering technique. 1. At 22 degrees C the radius of gyration of isolated human spectrin heterodimers in 0.1 M NaCl aqueous solution (pH 7.3) was found to be about 22 nm. 2. The radius of gyration of isolated human spectrin heterodimers was found to increase to about 40 nm as the ionic strength of the spectrin solution (pH 7.3) was reduced to about 1 mM. 3. The light scattering study indicates that the isolated human spectrin heterodimers were highly expanded and flexible molecules with a contour length exceeding about 140 nm.

Adult↗
PubMed1978

Human spectrin. II. An electro-optic study.

The electrically induced birefringence of human spectrin heterodimer solutions has been studied. 1. Human spectrin heterodimers were found to have a specific Kerr constant Bsp = +(5 +/- 2) . 10(-11) m4/(V2 . kg). 2. Human spectrin exhibited a birefringence relaxation time tau decay = (2.0 +/- 0.3) microseconds. 3. The electro-optic study indicates that human spectrin heterodimers have a contour length of more than 40--50 nm.

Birefringence↗
PubMed1978

A freeze-etch study of dense fibres in rat spermatozoa.

The presence of oblique striations on the cortex of the dense fibres of the rat spermatozoon is confirmed; they have a main periodicity of approximately 40 nm and a secondary one of about 20 nm. Disruption of spermatozoa by Triton X-100 and dithiothreitol and fixation in glutaraldehyde do not affect the pattern. The dense fibre cortex appears to consist of globular substructure units with a diameter of about 19 nm.

Animals↗
PubMed1977

Rotary replication for freeze-etching.

Rotary replication has been adapted to freeze-etching and evaluated using T4 polyheads, erythrocyte ghosts, and chloroplast membranes. Conventional electron microscopy, electron diffraction, and optical diffraction and filtering indicate that platinum-carbon rotary replication renders radially symmetrical contrast and 25 A resolution to freeze-etched specimens so as to clarify subunit structure not normally evident in unidirectional shadow replicas.

Carbon↗
PubMed1977

Intramembrane particle aggregation in erythrocyte membranes and band 3-lipid recombinants.

The low pH-induced aggregation of intramembrane particles in human erythrocyte membranes was studied in native membranes and in a reconstituted model system. A significant difference in such aggregation was found when samples of freshly prepared ghosts were compared to ghosts receiving pretreatments that removed most of spectrin-actin from underneath the membrane. All conditions effective in aggregating particles are equally effective in precipitating extracted mixtures of spectrin and actin. In Band 3-lipid recombinants, the pH-induced aggregation of particles was duplicated only in samples containing spectrin-actin that equilibrated with these recombinants in sucrose gradients. Therefore, it was proposed that spectrin-actin components, through their associations with the underlying intramembrane particles, could impede particle lateral mobility and also determine particle redistribution in erythrocyte membrane.

Actins↗
PubMed1976

Intramembrane particle aggregation in erythrocyte ghosts. II. The influence of spectrin aggregation.

Physicochemical properties of mixtures of spectrin and actin extracted from human erythrocyte ghosts have been correlated with ultrastructural changes observed in freeze-fractured erythrocyte membranes. (1) Extracted mixtures of spectrin and actin have a very low solubility (less than 30 mug/ml) near their isoelectric point, pH 4.8. These mixtures are also precipitated by low concentrations of Ca2+, Mg2+, polylysine or basic proteins. (2) All conditions which precipitate extracts of spectrin and actin also induce aggregation of the intramembrane particles in spectrin-depleted erythrocyte ghosts. Precipitation of the residual spectrin molecules into small patches on the cytoplasmic surface of the ghost membrane is thought to be the cause of particle aggregations, implying an association between the spectrin molecules and the intramembrane particles. (3) When fresh ghosts are exposed to conditions which precipitate extracts of spectrin and actin, only limited particle aggregation occurs. Instead, the contraction of the intact spectrin meshwork induced by the precipitation conditions compresses the lipid bilayer of the membrane, causing it to bleb off particle-free, protein-free vesicles. (4) The absence of protein in these lipid vesicles implies that all the proteins of the erythrocyte membrane are immobilized by association with either the spectrin meshwork or the intramembrane particles.

Actins↗