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

doi:10.1007/978-3-0348-8397-9_58

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 proceeding › Chapter 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 language	English
Title of host publication	Biochemistry and molecular biology of vitamin B₆ and PQQ-dependent proteins
Publisher	Birkhäuser Verlag
Pages	355-358
Number of pages	4
ISBN (Electronic)	9783034883979
ISBN (Print)	9783034895491
DOIs	https://doi.org/10.1007/978-3-0348-8397-9_58
Publication status	Published - 2000

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10.1007/978-3-0348-8397-9_58

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title = "Characterization of recombinant porcine pyridoxal kinase using surface plasmon resonance biosensor technique",

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.",

author = "C.C. Fong and W.P. Lai and M. Yang and Leung, {Yun Chung} and Wong, {Man Sau}",

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doi = "10.1007/978-3-0348-8397-9_58",

language = "English",

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Characterization of recombinant porcine pyridoxal kinase using surface plasmon resonance biosensor technique. / Fong, C.C.; Lai, W.P.; Yang, M. et al.
Biochemistry and molecular biology of vitamin B₆ and PQQ-dependent proteins. Birkhäuser Verlag, 2000. p. 355-358.

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

TY - CHAP

T1 - Characterization of recombinant porcine pyridoxal kinase using surface plasmon resonance biosensor technique

AU - Fong, C.C.

AU - Lai, W.P.

AU - Yang, M.

AU - Leung, Yun Chung

AU - Wong, Man Sau

PY - 2000

Y1 - 2000

N2 - 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.

AB - 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.

U2 - 10.1007/978-3-0348-8397-9_58

DO - 10.1007/978-3-0348-8397-9_58

M3 - Chapter in an edited book (as author)

SN - 9783034895491

SP - 355

EP - 358

BT - Biochemistry and molecular biology of vitamin B₆ and PQQ-dependent proteins

PB - Birkhäuser Verlag

ER -

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

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