Please use this identifier to cite or link to this item: http://hdl.handle.net/10397/54798
Title: Characterization of recombinant porcine pyridoxal kinase using surface plasmon resonance biosensor technique
Authors: Fong, CC
Lai, WP
Yang, M
Leung, YC 
Wong, MS 
Issue Date: 2000
Publisher: Birkhäuser Verlag
Source: In A Iriarte, M Martinez-Carrion & HM Kagan (Eds.), Biochemistry and molecular biology of vitamin B₆ and PQQ-dependent proteins, p. 355-358. Basel, Switzerland ; Boston: Birkhäuser Verlag, 2000 How to cite?
Abstract: In the present study, surface plasmon resonance biosensor was employed to characterize the binding interaction between wild type porcine Pyridoxal Kinase (PK) and an immobilized substrate, pyridoxamine. The binding of PK to the immobilized pyridoxamine was followed in real time and the kinetic parameters were derived from the sensorgram using the BlAevaluationTM software. At pH 7.4, the association rate constant and dissociation rate constant of the wild-type PK for immobilized pyridoxamine are 7.25 x 103±0.35 x 103M-1s-1 and 5.01 x 10-3±0.93 x 10-3s-1respectively. The equilibrium affinity constant of the wild-type PK is 1.45 x 106M-1. The effect of buffer pH on the binding kinetic parameters was also determined.
URI: http://hdl.handle.net/10397/54798
ISBN: 978-3-0348-9549-1 (print)
978-3-0348-8397-9 (online)
DOI: 10.1007/978-3-0348-8397-9_58
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