Polymerization defect of fibrinogen Baltimore III due to a γAsn308 → Ile mutation

Shanta Bantia, William R. Bell, Chi V. Dang

Research output: Contribution to journalArticle

Abstract

Fibrinogen Baltimore III, a congenital abnormal fibrinogen with impaired fibrin monomer polymerization, displays a normal γ-chain and a γ-variant that has an apparently lower relative molecular weight (mol wt) than normal on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Reverse phase high-performance liquid chromatography (HPLC) analysis of the lysyl endopeptidase digest of the purified 7-chains of fibrinogen Baltimore III revealed the presence of a peptide that is not found in the digest of the normal fibrinogen γ-chain. Amino acid sequence analysis of this peptide indicated that the γ-chain residue 308, asparagine. is replaced by isoleucine. Concanavalin A bound both normal and variant 7-chains of fibrinogen Baltimore III, indicating that the carbohydrate moiety is not altered and is not responsible for the increase in electrophoretic mobility of the Baltimore III 7-chain. This study suggests that the integrity of γAsn308 is critical for fibrin monomer polymerization, since alteration to either a basic (fibrinogen Kyoto I, Asn → Lys) or hydrophobic (Asn → Ile) residue results in significantly delayed polymerization of fibrinogen to fibrin.

Original languageEnglish (US)
Pages (from-to)1659-1663
Number of pages5
JournalBlood
Volume75
Issue number8
StatePublished - Apr 15 1990

ASJC Scopus subject areas

  • Hematology

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    Bantia, S., Bell, W. R., & Dang, C. V. (1990). Polymerization defect of fibrinogen Baltimore III due to a γAsn308 → Ile mutation. Blood, 75(8), 1659-1663.