Characterization of recombinant porcine pyridoxal kinase using surface plasmon resonance biosensor technique

C.C. Fong, W.P. Lai, M. Yang, Yun Chung Leung, Man Sau Wong

Research output: Chapter in book / Conference proceedingChapter in an edited book (as author)Academic research

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.
Original languageEnglish
Title of host publicationBiochemistry and molecular biology of vitamin B₆ and PQQ-dependent proteins
PublisherBirkhäuser Verlag
Pages355-358
Number of pages4
ISBN (Electronic)9783034883979
ISBN (Print)9783034895491
DOIs
Publication statusPublished - 2000

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