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. 1974 Mar 1;60(3):541–553. doi: 10.1083/jcb.60.3.541

THE EFFECTS OF THROMBIN ON PHYTOHEMAGGLUTININ RECEPTOR SITES IN HUMAN PLATELETS

John R Feagler 1, Thomas W Tillack 1, David D Chaplin 1, Philip W Majerus 1
PMCID: PMC2109233  PMID: 4207395

Abstract

We have previously demonstrated that lentil phytohemagglutinin (lentil-PHA) binds to human platelet membranes without causing either aggregation or the release reaction. When platelets are treated with thrombin, there is an increase in lentil-PHA binding suggesting the appearance of new receptor sites on the cell surface. We prepared a lentil-PHA-ferritin conjugate using affinity chromatography which was used to saturate cell surface receptor sites. Studies using this conjugate suggest that thrombin causes a complex change in the platelet surface involving a decrease in the number of lentil-PHA receptor sites on the external platelet surface with a marked increase in sites within the center of the canalicular system. These increased sites may result from fusion of granule membranes with the canalicular membranes during the secretion process. There is no obvious relationship between lentil-PHA receptor sites and intramembranous particles.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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