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Investigation of non-covalent interactions of amyloidogenic human lysozyme variants and camelid antibodies

Abstract:
The investigation of non-covalent interactions of amyloidogenic human lysozyme variants and camelid antibodies was discussed. The two naturally occuring human lysozyme variants were implicated in hereditary systemic amyloidosis. Tri-NAG was shown to bind to both free and associated lysozyme, implying that the enzyme was still active when bound to the antibody. The single-domain camelid antibody appears to bind with its antigen lysozyme and the variants thereof with a 1:1 stoichiometry. Amyloidogenic lysozyme variants undergo a spontaneous cooperative unfolding event in solution which was detectable around pH8.05.

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Host title:
Proceedings 50th ASMS Conference on Mass Spectrometry and Allied Topics
Pages:
253-254
Publication date:
2002-01-01


Pubs id:
pubs:282194
UUID:
uuid:ec3c5ab7-42d5-476f-8830-723140634e6d
Local pid:
pubs:282194
Source identifiers:
282194
Deposit date:
2013-09-17
ARK identifier:

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