Ionic properties of membrane association by vitamin K-dependent proteins: the case for univalency.
McDonald, J F
Ionic properties of membrane association by vitamin K-dependent proteins: the case for univalency. [electronic resource] - Biochemistry Dec 1997 - 15589-98 p. digital
Publication Type: Journal Article; Research Support, U.S. Gov't, P.H.S.
0006-2960
10.1021/bi971114z doi
Amino Acid Sequence
Animals
Blood Proteins--chemistry
Calcium--metabolism
Cattle
Electrochemistry
Enzyme Inhibitors--pharmacology
Factor V--metabolism
Hydrogen-Ion Concentration
Kinetics
Liposomes--chemistry
Models, Molecular
Molecular Sequence Data
Osmolar Concentration
Peptides--pharmacology
Phospholipids--chemistry
Protein Kinase C--antagonists & inhibitors
Prothrombin--chemistry
Scattering, Radiation
Sodium Chloride--pharmacology
Thermodynamics
Vitamin K--metabolism
Ionic properties of membrane association by vitamin K-dependent proteins: the case for univalency. [electronic resource] - Biochemistry Dec 1997 - 15589-98 p. digital
Publication Type: Journal Article; Research Support, U.S. Gov't, P.H.S.
0006-2960
10.1021/bi971114z doi
Amino Acid Sequence
Animals
Blood Proteins--chemistry
Calcium--metabolism
Cattle
Electrochemistry
Enzyme Inhibitors--pharmacology
Factor V--metabolism
Hydrogen-Ion Concentration
Kinetics
Liposomes--chemistry
Models, Molecular
Molecular Sequence Data
Osmolar Concentration
Peptides--pharmacology
Phospholipids--chemistry
Protein Kinase C--antagonists & inhibitors
Prothrombin--chemistry
Scattering, Radiation
Sodium Chloride--pharmacology
Thermodynamics
Vitamin K--metabolism