Hemophilia A due to mutations that create new N-glycosylation sites

Ashraf M. Aly, Miyoko Higuchi, Carol K. Kasper, Haig Kazazian, Stylianos E. Antonarakis, Leon W. Hoyer

Research output: Contribution to journalArticle

Abstract

In studying the molecular defects responsible for cross-reacting material-positive hemophilia A, we have identified two patients in whom the nonfunctional factor VIII-like protein has abnormal, slower-moving heavy or light chains on SDS/PAGE. Both patients have severe hemophilia A (

Original languageEnglish (US)
Pages (from-to)4933-4937
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume89
Issue number11
StatePublished - 1992

Fingerprint

Hemophilia A
Glycosylation
Mutation
Factor VIII
Polyacrylamide Gel Electrophoresis
Light
Proteins

Keywords

  • Denaturing gradient gel electrophoresis
  • Factor VIII
  • N-glycanase

ASJC Scopus subject areas

  • Genetics
  • General

Cite this

Hemophilia A due to mutations that create new N-glycosylation sites. / Aly, Ashraf M.; Higuchi, Miyoko; Kasper, Carol K.; Kazazian, Haig; Antonarakis, Stylianos E.; Hoyer, Leon W.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 89, No. 11, 1992, p. 4933-4937.

Research output: Contribution to journalArticle

Aly, Ashraf M. ; Higuchi, Miyoko ; Kasper, Carol K. ; Kazazian, Haig ; Antonarakis, Stylianos E. ; Hoyer, Leon W. / Hemophilia A due to mutations that create new N-glycosylation sites. In: Proceedings of the National Academy of Sciences of the United States of America. 1992 ; Vol. 89, No. 11. pp. 4933-4937.
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