BIACORE data processing: An evaluation of the global fitting procedure

被引：40

作者：

Ben Khalifa, M

Choulier, L

Lortat-Jacob, H

Altschuh, D

Vernet, T

机构：

[1] Univ Grenoble 1, CEA, CNRS UMR 5075,Lab Ingn Macromol, Inst Biol Struct Jean Pierre Ebel, F-38027 Grenoble 1, France

[2] Univ Grenoble 1, CEA, CNRS UMR 5075,Lab Biophys Mol, Inst Biol Struct Jean Pierre Ebel, F-38027 Grenoble 1, France

[3] CNRS, Inst Biol Mol & Cellulaire, UPR 9021, F-67084 Strasbourg, France

来源：

ANALYTICAL BIOCHEMISTRY | 2001年 / 293卷 / 02期

关键词：

BIACORE; molecular interactions; binding kinetics; numerical integration; surface plasmon resonance; biosensor; mass transport; complex binding;

D O I：

10.1006/abio.2001.5119

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Data from real-time molecular interaction analysis using BIACORE are currently evaluated by numerical integration. We have investigated the ability of two software packages (BLCevaluation 3.0 and CLAMP99) to analyze complex interactions. Three experimental data sets of high quality obtained with BIACORE upgraded and 2000 instruments, representative of simple bimolecular, heterogeneous ligand, and mass-transport-limited interactions, were processed by the global fitting procedure. The two software, which differ mainly in the statistical assessment of the output values,:were able to discriminate correctly between various interacting models and provided very close output parameters with satisfactory statistical tests. (C) 2001 Academic Press.

引用

页码：194 / 203

页数：10

共 32 条

[1] DETERMINATION OF KINETIC CONSTANTS FOR THE INTERACTION BETWEEN A MONOCLONAL-ANTIBODY AND PEPTIDES USING SURFACE-PLASMON RESONANCE [J].

ALTSCHUH, D ;

DUBS, MC ;

WEISS, E ;

ZEDERLUTZ, G ;

VANREGENMORTEL, MHV .

BIOCHEMISTRY, 1992, 31 (27) :6298-6304

[2]

BEECHEM JM, 1992, METHOD ENZYMOL, V210, P37

[3]

Ben Khalifa M, 2000, J MOL RECOGNIT, V13, P127

[4] Functional mapping of conserved residues located at the VL and VH domain interface of a Fab [J].

Chatellier, J ;

VanRegenmortel, MHV ;

Vernet, T ;

Altschuh, D .

JOURNAL OF MOLECULAR BIOLOGY, 1996, 264 (01) :1-6

[5] Real-time kinetic studies on the interaction of transforming growth factor α with the epidermal growth factor receptor extracellular domain reveal a conformational change model [J].

De Crescenzo, G ;

Grothe, S ;

Lortie, R ;

Debanne, MT ;

O'Connor-McCourt, M .

BIOCHEMISTRY, 2000, 39 (31) :9466-9476

[6]

FISHER RJ, 1994, PROTEIN SCI, V3, P257

[7] BIAcore for macromolecular interaction [J].

Fivash, M ;

Towler, EM ;

Fisher, RJ .

CURRENT OPINION IN BIOTECHNOLOGY, 1998, 9 (01) :97-101

[8] Binding kinetics of an antibody against HIV p24 core protein measured with real-time biomolecular interaction analysis suggest a slow conformational change in antigen p24 [J].

Glaser, RW ;

Hausdorf, G .

JOURNAL OF IMMUNOLOGICAL METHODS, 1996, 189 (01) :1-14

[9] IMMOBILIZATION OF PROTEINS TO A CARBOXYMETHYLDEXTRAN-MODIFIED GOLD SURFACE FOR BIOSPECIFIC INTERACTION ANALYSIS IN SURFACE-PLASMON RESONANCE SENSORS [J].

JOHNSSON, B ;

LOFAS, S ;

LINDQUIST, G .

ANALYTICAL BIOCHEMISTRY, 1991, 198 (02) :268-277

[10]

JONSSON U, 1991, BIOTECHNIQUES, V11, P620

← 1 2 3 4 →