Blood Coagulation Factor IX Residues Glu78 and Arg94 Provide a Link between Both Epidermal Growth Factor-like Domains That Is Crucial in the Interaction with Factor VIII Light Chain
Open Access
- 1 January 1998
- journal article
- Published by Elsevier
- Vol. 273 (1) , 222-227
- https://doi.org/10.1074/jbc.273.1.222
Abstract
No abstract availableKeywords
This publication has 25 references indexed in Scilit:
- Ca2+ Binding to the First Epidermal Growth Factor-like Domain of Human Blood Coagulation Factor IX Promotes Enzyme Activity and Factor VIII Light Chain BindingPublished by Elsevier ,1996
- The Sequence Glu1811-Lys1818 of Human Blood Coagulation Factor VIII Comprises a Binding Site for Activated Factor IXPublished by Elsevier ,1996
- The structure of a Ca2+-binding epidermal growth factor-like domain: Its role in protein-protein interactionsCell, 1995
- The Role of Cleavage of the Light Chain at Positions Arg1689 or Arg1721 in Subunit Interaction and Activation of Human Blood Coagulation Factor VIIIPublished by Elsevier ,1995
- Calcium-dependent interactions between Gla and EGF domains in human coagulation factor IXBiochemistry, 1994
- Epidermal growth factor-like modulesCurrent Opinion in Structural Biology, 1993
- The coagulation cascade: initiation, maintenance, and regulationBiochemistry, 1991
- Complete nucleotide sequences of the gene for human factor IX (antihemophilic factor B)Biochemistry, 1985
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976
- PEROXIDASE-LABELED ANTIBODY A NEW METHOD OF CONJUGATIONJournal of Histochemistry & Cytochemistry, 1974