NH sub(2)-terminal globular domain of human platelet glycoprotein Ib alpha has a methionine super(145)/threonine super(145) amino acid polymorphism, which is associated with the HPA-2 (Ko) alloantigens
The glycoprotein (GP) Ib/IX complex, a prominent platelet GP complex, is the primary receptor for vWF. Previously, we have established that an antigenic polymorphism of platelets, the HPA-2 or Ko alloantigen system, is located on the 45-kD amino-terminal globular domain of GPIb alpha . With the poly...
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Published in: | The Journal of clinical investigation Vol. 89; no. 2; pp. 381 - 384 |
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Main Authors: | , , , , |
Format: | Journal Article |
Language: | English |
Published: |
01-01-1992
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Online Access: | Get full text |
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Summary: | The glycoprotein (GP) Ib/IX complex, a prominent platelet GP complex, is the primary receptor for vWF. Previously, we have established that an antigenic polymorphism of platelets, the HPA-2 or Ko alloantigen system, is located on the 45-kD amino-terminal globular domain of GPIb alpha . With the polymerase chain reaction, we have amplified two segments of the GPIb alpha gene coding for the first 382 amino acids of two HPA-2a and two HPA-2b homozygous individuals. DNA-typing for the HPA-2 alloantigen system on genomic DNA obtained from a small number of cells may be applied for determining the genotype of a fetus from an immunized mother or of severely thrombocytopenic patients. |
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Bibliography: | ObjectType-Article-2 SourceType-Scholarly Journals-1 content type line 23 ObjectType-Feature-1 |
ISSN: | 0021-9738 |