Treatment of human muscle creatine kinase with glutaraldehyde preferentially increases the immunogenicity of the native conformation and permits production of high-affinity monoclonal antibodies which recognize two distinct surface epitopes
- 1 December 1989
- journal article
- research article
- Published by Elsevier in Journal of Immunological Methods
- Vol. 125 (1-2) , 251-259
- https://doi.org/10.1016/0022-1759(89)90100-2
Abstract
No abstract availableThis publication has 16 references indexed in Scilit:
- Monoclonal antibody studies of creatine kinase. The ART epitope: evidence for an intermediate in protein foldingBiochemical Journal, 1989
- Monoclonal antibody studies of creatine kinase. Antibody-binding sites in the N-terminal region of creatine kinase and effects of antibody on enzyme refoldingBiochemical Journal, 1987
- Isolation and sequence analysis of a full-length cDNA for human M creatine kinaseBiochemical and Biophysical Research Communications, 1986
- Monoclonal-antibody studies of creatine kinase. The proteinase K-cleavage siteBiochemical Journal, 1985
- A monoclonal antibody to human brain-type creatine kinase. Increased avidity with mercaptansBiochemical Journal, 1983
- Immunoassay of muscle-specific creatine kinase with a monoclonal antibody and application to myogenesis and muscular dystrophyBiochemical Journal, 1983
- A monoclonal antibody against the skeletal muscle enzyme, creatine kinaseFEBS Letters, 1982
- [9] Methods for the preparation of enzyme-antibody conjugates for use in enzyme immunoassayPublished by Elsevier ,1981
- Creatine kinase isoenzymes in the assessment of heart diseaseAmerican Heart Journal, 1978
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970