Comparison of the Secondary Structures and Binding Sites of C-Reactive Protein and the Phosphorylcholine-Binding Murine Myeloma Proteins

摘要: The circular dichroism (C.D.) spectrum of C-reactive protein in the 200- to 240-nm region indicates that has a) a considerable content α-helix, feature not found immunoglobulins, and, b) very similar structure amyloid P component. In 240- 320-nm two proteins have different CD spectra, and show little resemblance phosphorylcholine-binding murine myeloma such as MOPC 167 IgA. Removal calcium from produced large change attributable tyrosine, addition phosphorylcholine small same region. Inhibition reaction with pneumococcal C substance by analogs showed is much more specific for phosphate moiety than proteins. Despite these structural binding-site differences, comparison amino-acid sequences hypervariable regions suggests sites may still features common.