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Investigation of C4bC2 complex formation by surface plasmon resonance by A. Laich; R.B. Sim is a Immunology and Microbiology article available to read on EtoBox.

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Complex formation between the complement proteins C4b and C2 was investigated by surface plasmon resonance. lmmobilisation of C4b or C4(H20) by amine coupling was optimised at pH 5.0. C4b-C2 interaction was measured at ionic strengths form 30-830mM NaCl and in &15mM MgClp. Maximum binding was observed at 30mM NaCI. and was negligible above 300mM NaCI. C4b-C2 affinity K. was determined by steady state analysis to be 7.17~1o'~M in physiological conditions. Ca\*' is not required for formation of the complex, as experiments in presence EGTA gave a similar KD of 7.7Oxlo"M. For C4(H20)-C2 complex formation, a Kc of 4.03xlo"M was calculated. Consistent with previous reports, C4b-C2 binding, is a multi-phasic interaction. It was observed that about 5% of complexes did not decay. It is possible that the abnormal dissociation behaviour is due to aggregation of small proportions of C2 during storage. Although the formation of C4b-C2 complexes is reported to be Mg"-dependent, complex formation in presence of EDTA was observed. Binding in EDTA showed characteristics of a monophasic interaction and had a very slow dissociation rate constant (k.,) of 2.5~10'~~". It is possible that the observed s

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Author

A. Laich; R.B. Sim

Publisher

Elsevier Science; Elsevier ; Elsevier BV (ISSN 0162-3109)

Published

2000

Language

EN

Field

Immunology and Microbiology (Life Sciences)