Demonstration of a new glycoprotein Ib-related component in platelet extracts prepared in the presence of leupeptin
| Autor: | Nils Olav Solum, Terje Olsen, Inger Hagen, Frank Brosstad, G.O. Gogstad |
|---|---|
| Rok vydání: | 1983 |
| Předmět: |
Blood Platelets
Platelet Aggregation Leupeptins Octoxynol Detergents Biophysics Platelet Membrane Glycoproteins Immunoelectrophoresis Platelet membrane glycoprotein Biochemistry Polyethylene Glycols chemistry.chemical_compound medicine Animals Humans Platelet Glycoproteins Gel electrophoresis Factor VIII biology medicine.diagnostic_test Leupeptin Membrane Proteins Platelet Glycoprotein GPIb-IX Complex Cell Biology Molecular Weight Agglutination (biology) Solubility Glycoprotein Ib chemistry biology.protein Cattle Electrophoresis Polyacrylamide Gel Immunoelectrophoresis Two-Dimensional Oligopeptides |
| Zdroj: | Biochimica et Biophysica Acta (BBA) - Biomembranes. 729:53-61 |
| ISSN: | 0005-2736 |
| Popis: | The water-soluble protein glycocalicin is generated during platelet lysis by a proteolytic attack on the integral membrane glycoprotein GP Ib. However, only small amounts of glycocalicin are formed when platelets are solubilized by 1% Triton X-100. Crossed immunoelectrophoresis of such extracts using an antiserum to glycocalicin, shows a continuous immunoprecipitate consisting of two peaks, one representing glycocalicin and the other GP Ib. When leupeptin was present during solubilization, subsequent immunoelectrophoresis revealed yet another GP Ib-related component represented by a third, slow-migrating peak of the immunoprecipitate. During incubation of platelets with dibucaine followed by solubilization in the presence of leupeptin, a gradual transformation of this new form of GP Ib into the previously defined one took place prior to the formation of glycocalicin. An increase followed by a decrease in the agglutination response of the platelets to bovine von Willebrand factor occurred concomitant with these transformations. SDS-polyacrylamide gel electrophoresis of Triton X-100 extracts of platelets did not reveal any difference in the size of GP Ib whether or not leupeptin had been present during the solubilization. |
| Databáze: | OpenAIRE |
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