title: Mechanism of Na(+) binding to thrombin resolved by ultra-rapid kinetics.
abstract: The interaction of Na(+) and K(+) with proteins is at the basis of numerous processes of biological importance. However, measurement of the kinetic components of the interaction has eluded experimentalists for decades because the rate constants are too fast to resolve with conventional stopped-flow methods. Using a continuous-flow apparatus with a dead time of 50 micro s we have been able to resolve the kinetic rate constants and entire mechanism of Na(+) binding to thrombin, an interaction that is at the basis of the procoagulant and prothrombotic roles of the enzyme in the blood.
authors.affiliation: Istituto di Biologia e Patologia Molecolari del CNR, Dipartimento di Scienze Biochimiche, Universita' di Roma La Sapienza, Rome, Italy. stefano.gianni@uniroma1.it
authors.forename: Stefano
authors.initials: S
authors.lastname: Gianni
authors.forename: Ylva
authors.initials: Y
authors.lastname: Ivarsson
authors.forename: Alaji
authors.initials: A
authors.lastname: Bah
authors.forename: Leslie A
authors.initials: LA
authors.lastname: Bush-Pelc
authors.forename: Enrico
authors.initials: E
authors.lastname: Di Cera
mesh_terms: D006801:Humans; D007700:Kinetics; D009154:Mutation; D012964:Sodium / Q000737:chemistry*; D013917:Thrombin / Q000737:chemistry* / Q000235:genetics
chemical_list: D012964:Sodium; D013917:Thrombin