Subcellular Localization of a Glycoprotein Released from Human Platelets upon Stimulation by Thrombin
The treatment of washed, intact human blood platelets with 1 U/ml of thrombin for 5 min at 37 °C is linked to the disappearance from the particulate fraction of the homogenized cells of a protein band discernible in the SDS-polyacrylamide gel electrophoresis pattern of untreated platelets. Accordin...
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| Main Authors: | , , |
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| Format: | Article |
| Language: | deu |
| Published: |
Swiss Chemical Society
1976-02-01
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| Series: | CHIMIA |
| Online Access: | https://www.chimia.ch/chimia/article/view/9291 |
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| Summary: | The treatment of washed, intact human blood platelets with 1 U/ml of thrombin for 5 min at 37 °C is linked to the disappearance from the particulate fraction of the homogenized cells of a protein band discernible in the SDS-polyacrylamide gel electrophoresis pattern of untreated platelets. Accordingly, this material was termed thrombin sensitive protein (TSP) by its discoverers, who also presented evidence that TSP is a glycoprotein of a molecular weight of 190,000.
The present work describes the localization of TSP in human platelets. TSP is not a membrane constituent, but associated with orgenelle fractions in the region of higher densities. It therefore is not, as originally suggested, a direct substrate for thrombin on the platelet surface, but takes part in the platelet release reaction upon a variety of external stimuli. An apparent molecular weight of 150,000 was found for TSP; this value coincides with the one reported for so-called glycoprotein I, which, different from TSP, is a membrane constituent.
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| ISSN: | 0009-4293 2673-2424 |