Immunochemical Properties of Rabbit Antibody Fragments to Taka-amylase A

Abstract

Rabbit anti-TAA γ-globulin was digested with papain and reduced with mercapto-ethanol. In this report, the immunochemical properties of rabbit anti-TAA fragments obtained by these methods were studied, and following results were obtained.
1) Anti-TAA activity of F-1 of papain digest was much less than that of F-II, although no remarkable difference was observed in their amino acid contents,
2) Maltosidase activity of TAA was increased by papain digests of anti-TAA, and the increase of maltosidase activity by F-I was higher than that by F-II. These data indicate the immunochmical differences between F-I and F-II of anti-TAA, and some interpretations and speculation of the mechanisms which give such differences are proposed.
3) The chain A fraction from reduced anti-TAA seemed to have some of immunological activities of anti-TAA. However, there exists a possibility that the activities of the chain A fraction might be derived in part from possible contaminations of unreduced and reconstituted anti-TAA.
4) The chain B fraction from reduced anti-TAA had no immunological activity.