Fibrinogen Lima: a homozygous dysfibrinogen with an A alpha-arginine-141 to serine substitution associated with extra N-glycosylation at A alpha-asparagine-139. Impaired fibrin gel formation but normal fibrin-facilitated plasminogen activation catalyzed by tissue-type plasminogen activator.

An A alpha-arginine-141 to serine substitution has been identified in a homozygous dysfibrinogen, fibrinogen Lima, associated with impaired fibrin polymerization. The point mutation created an asparagine-X-serine-type glycosylation sequence, and indeed, extra, mainly disialylated biantennary oligosa...

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Main Authors: Maekawa, H, Yamazumi, K, Muramatsu, S, Kaneko, M, Hirata, H, Takahashi, N, Arocha-Piñango, C L, Rodriguez, S, Nagy, H, Perez-Requejo, J L
Formáid: Artigo
Teanga:Inglês
Foilsithe: 1992
Ábhair:
Research Article
Rochtain Ar Líne:https://ncbi.nlm.nih.gov/pmc/articles/PMC443064/
https://ncbi.nlm.nih.gov/pubmed/1634621
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