Biomedical subjects

M O Spycher

Publications and source records attributed to M O Spycher.

20 records · Page 2Linked to original sources

PubMed1983

[Binding of IgG and its aggregates to human platelets can be made saturable by using deoxyglucose and antimycin A].

Binding of bisdiazoniumbenzidine cross-linked (BDB) and monomeric IgG to washed human platelets at 37 degrees C was assessed. Metabolic inhibitors and prostaglandin E1 permitted study of partially reversible and saturable binding of the ligands to platelets: in presence of 0.25 microM antimycin A and 6 mM deoxyglucose, maximal binding of 3H-BDB-IgG (10 min, 37 degrees C) was 0.52 fg per platelet and of 3H-IgG (20 min, 37 degrees C) 0.13 fg per platelet. In presence of 6 mM glucose, however, the amount of IgG bound per platelet was higher and not saturable. These findings suggest that IgG is actively engulfed by the platelets.

Antimycin A↗

PubMed1982

Surface labeling of human platelets by reductive methylation.

A simple, reproducible method for the specific labeling of the surface proteins of human platelets with tritium is described. The labeled platelets were analyzed by two-dimensional gel electrophoresis (isoelectric focusing/sodium dodecyl sulfate-polyacrylamide gel electrophoresis) followed by fluorography and the results compared with those obtained by conventional methods. Reductive methylation gave an intense labeling of membrane glycoproteins. There was no cross-linking of the labeled membrane proteins by formaldehyde nor could clear evidence be found that inner proteins were labeled by permeation of the reagents through the plasma membrane. As well as previously described platelet membrane glycoproteins, several others could be detected that were not invariable seen using labeling techniques.

Actins↗