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Biomedical subjects

W Linss

Publications and source records attributed to W Linss.

At least 109 records · Page 6Linked to original sources
PubMed1976

Inverse localization of Ca2+ and La3+ high affinity binding sites of the red cell membrane.

Glutaraldehyde fixation in the presence of both 90 mM La3+ resulted in opaque deposits were also seen in specimens fixed in a glutaraldehyde-CaCl2 medium devoid of La3+. In that case only small amounts of a moderately opaque substance had accumulated or remained at the external surface of the erythrocyte membrane. Specimens previously fixed with Ca2+, La3+ supplemented glutaraldehyde lost their internal deposits completely during postifixation with OsO4. The findings provide evidence of Ca2+ high affinity binding sites at the internal surface of the erythrocyte membrane presumably identical with the filamentous matrix. Glycocalyx constituents are considered external Ca2+ low affinity binding sites, however, capable of accumulating high amounts of La3+ during glutaraldehyde fixation.

Binding Sites↗
PubMed1976

Calcium binding to the erythrocyte membrane.

Calcium binding sites of human red blood cells were localized by means of a method according to OSCHMAN and WALL (1972). The procedure resulted in multiple opaque deposits at the inner surface of the erythrocyte membrane.

Binding Sites↗
PubMed1975

[Studies on the osmotic resistance and the viability of amidinated erythrocytes].

The present studies are concerned with properties of amidinated erythrocytes. The reactions of dimethyladipimidate with proteins in solution and red blood cells, respectively, result in an intermolecular cross-linking. Following an amidination of human serum albumin or human gamma-globulin cross-linked products of increased molecular weight have been demonstrated by polyacrylamide gel and immune electrophoresis. Human erythrocytes previously amidinated intensely, exhibit a restricted motility of membrane particles and cross-linked hemoglobin. Intensely amidinated erythrocytes are resistant against distilled water, and they do no longer agglutinate. The findings presumably indicate an increased permeability of the amidinated red cell membrane. The glycolytic activity was found to be normal in moderately amidinated erythrocytes. In comparison with normal red blood cells, previously moderately amidinated erythrocytes of the rat become sequestered more quickly after re-injection into the vascular system.

Amidines↗
PubMed1975

Porosity and surface area of anionic resins: limitations in the employment of model substrates for the colloidal iron reaction.

Quantitative evaluations of the uptake of an acid ferric hydroxide sol revealed the iron binding of model substrates unrelated to their ion binding capacity. Electron microscopy showed iron particles bound exclusively or mainly to the surfaces of model substrates. Morphometric estimations resulted in a good agreement of the surface/volume ratio with the amount of bound iron. The results are discussed with regard to the steric hindrance of the colloidal iron reaction resulting in a nonstoichiometric interaction.

Anion Exchange Resins↗
PubMed1974

Digitonin induced rearrangement of membrane constituents of aldehyde fixed erythrocytes.

The present study demonstrates an altered distribution pattern of anionic sites of the human erythrocyte glycocalyx. The findings prove a significant rearrangement of membrane constituents induced by a digitonin treatment of aldehyde fixed red blood cells. The effect is not confined to lipids and, presumably, it causes the loss of lipidic and nonlipidic membrane components. It can be deduced that the fixation with a mixture of formaldehyde and glutaraldehyde insufficiently stabilizes the membrane structure.

Anions↗