Abstract
Antibodies are globular glycoproteins that protect animals from microbial and toxic insult. These proteins have proven to have substantial commercial and research value but are variably susceptible to freeze-thaw damage, thus limiting their usefulness. Several carbohydrates and divalent cations were examined alone and in combination to determine whether they could protect antibody from freeze-thaw damage. The amino acid proline was also tested. Two antibodies, derived from different sources and specific for different antigens, were tested by a direct enzyme-linked immunosorbent assay (ELISA). Confirmation of antibody freeze-lability was obtained by rocket electrophoresis and radial immunodiffusion tests. Neither carbohydrate nor divalent cation alone fully protected antibody activity from freeze-thaw damage. However, several combinations protected antibody activity completely when compared to their effect on antibody maintained at room temperature. In the case of affinity-purified antibody, full protection of antibody activity relative to an untreated control was obtained. In several instances, cryoprotection of antibody by solute-divalent cation combinations was synergistic and not an additive effect of each component. Alkaline phosphatase, an enzyme typically linked to antibody for an ELISA, was not freeze-thaw labile. These results indicate that antibody function can be fully protected from damage due to freeze-thaw treatment by organic solutes in combination with divalent cations.
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