Effects of limited denaturation by heat on the dynamic conformation of equine immunoglobulin M antibody and on interaction with antigen and complement.
Abstract: No abstract available
Publication Date: 1981-01-06 PubMed ID: 6781534DOI: 10.1021/bi00504a032Google Scholar: Lookup
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- Journal Article
- Research Support
- U.S. Gov't
- P.H.S.
Cite This Article
APA
Siegel RC, Cathou RE.
(1981).
Effects of limited denaturation by heat on the dynamic conformation of equine immunoglobulin M antibody and on interaction with antigen and complement.
Biochemistry, 20(1), 192-198.
https://doi.org/10.1021/bi00504a032 Publication
Researcher Affiliations
MeSH Terms
- Animals
- Antigen-Antibody Complex
- Antigens
- Circular Dichroism
- Complement C1
- Complement Fixation Tests
- Dansyl Compounds
- Horses
- Immunoglobulin Fab Fragments
- Immunoglobulin M
- Immunoglobulin mu-Chains
- Protein Conformation
- Protein Denaturation
Grant Funding
- AI-10115 / NIAID NIH HHS
Citations
This article has been cited 2 times.- Shulman MJ, Heusser C, Filkin C, Köhler G. Mutations affecting the structure and function of immunoglobulin M.. Mol Cell Biol 1982 Sep;2(9):1033-43.
- Shulman MJ, Pennell N, Collins C, Hozumi N. Activation of complement by immunoglobulin M is impaired by the substitution serine-406----asparagine in the immunoglobulin mu heavy chain.. Proc Natl Acad Sci U S A 1986 Oct;83(20):7678-82.
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