| Autor: |
Mustard, JF, Kinlough-Rathbone, RL, Packham, MA, Perry, DW, Harfenist, EJ, Pai, KR |
| Zdroj: |
Blood; November 1979, Vol. 54 Issue: 5 p987-993, 7p |
| Abstrakt: |
Although 125I-fibrinogen becomes associated with washed platelets from normal human subjects during ADP-induced shape change and aggregation, 125I-fibrinogen did not become associated with washed plateletes from a thrombasthenic subject during ADP-induced shape change and the platelets did not aggregate. Platelets from control and thrombasthenic subjects were treated with chymotrypsin, which is known to degrade platelet membrane glycoproteins. More 125I-fibrinogen became associated with chymotrypsin-pretreated platelets from normal subejcts than with untreated platelets, and fibrinogen caused the enzyme-treated platelets to aggregate. 125I-fibrinogen did not become associated with chymotrypsin-pretreated thromobasthenic platelets, and fibrinogen did not aggregate them. Thus, there appears to be a defect in thrombasthenic platelets that prevents the association of fibrinogen with them. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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