Structural changes of fibrinogen molecule mediated by the N-homocysteinylation reaction

Homocysteine and its cyclic ester homocysteine thiolactone (HTL) have been involved in the detrimental consequences associated to hyperhomocysteinemia, an independent risk factor for vascular diseases. HTL reacts with protein lysine residues in a process named N-homocysteinylation. The aim of our st...

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Detalles Bibliográficos
Autores principales: Genoud, V., Quintana, P.G., Gionco, S., Baldessari, A., Quintana, I.
Formato: JOUR
Materias:
Electrophoretic methods
Fibrinogen
Homocysteine-thiolactone hydrolysis
N-homocysteinylation
Proton nuclear magnetic resonance
fibrinogen
homocysteine
homocysteine thiolactone
mercaptoethanol
thiol group
Article
biochemical recurrence
capillary isoelectric focusing
capillary zone electrophoresis
controlled study
disulfide bond
homocysteinylation
hydrolysis
in vitro study
molecular stability
pH
polyacrylamide gel electrophoresis
priority journal
protein modification
protein structure
proton nuclear magnetic resonance
analogs and derivatives
capillary electrophoresis
chemistry
human
hyperhomocysteinemia
isoelectric focusing
metabolism
pathology
two dimensional gel electrophoresis
Electrophoresis, Capillary
Electrophoresis, Gel, Two-Dimensional
Homocysteine
Humans
Hydrogen-Ion Concentration
Hydrolysis
Hyperhomocysteinemia
Isoelectric Focusing
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_09295305_v45_n1_p66_Genoud
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

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