Date on Senior Honors Thesis
5-2016
Document Type
Senior Honors Thesis
Department
Chemistry
Degree Program
College of Arts and Sciences
Author's Keywords
fibrinogen; Factor XIII; coagulation; MALDI-TOF mass spectroscopy; NMR
Abstract
Formation of a stable thrombus in vivo depends on the interaction between fibrinogen and the transglutaminase factor XIII (FXIII). Characteristics of blood plasma, such as concentration of Ca2+, are well known to regulate the activation and subsequent reactivity of FXIII. Despite this knowledge, the role fibrin(ogen) plays in modulating FXIII activation and reactivity is not entirely delineated. Currently, the coagulation substrate fibrinogen Aα is proposed to contain a binding site for the active factor XIII with fibrinogen Aα E396 serving a major role. A series of mass spectrometry and NMR spectroscopy studies was conducted to assess whether putative interactions between residues 389-403 within Fbg Aα and FXIII influence the ability of FXIII A2 * to crosslink reactive residues within recombinant Fbg αA 233-425. Results indicate the electrostatic interaction of Fbg αA E396 with FXIII does not appreciably influence either the activation of FXIII A2 to FXIII A2 * or the ability of FXIII A2 * to recognize and bind to the substrate Fbg αA 233-425 and catalyze the crosslinking reaction.
Recommended Citation
Stephens, Chad A., "Evaluating the role that a putative FXIII binding site plays in the reactivity of three glutamines within the coagulation substrate Fibrinogen Aα (233-425)." (2016). College of Arts & Sciences Senior Honors Theses. Paper 123.
http://doi.org/10.18297/honors/123
