Isolation and characterization of adenosine deaminase in the adductor muscle of marine bivalve molluscs

Abstract

Adenosine deaminase was purified from the adductor muscles of the scallop Patinopecten yessoensis and the round clam Mactra chinensis to apparent homogeneity as judged by sodium dodecylsulfate-polyacrylamide gel electrophoresis (SDS-PAGE). SDS-PAGE and gel filtration showed that the enzymes were monomers with a molecular weight of 40000-43000. The optimum pH was in a slight alkaline range. The enzymes were active for adenosine and 2'-deoxyadenosine, but not for adenine, 5'-deoxyadenosine, or phosphorylated adenosines. The size, optimum pH, and substrate specificity of the purified enzymes were similar to those of adenosine deaminase in vertebrates. The antisera against adenosine deaminase from the adductor muscles of the scallop were cross-reactive with calf intestine adenosine deaminase as well as adenosine deaminase from the round clam adductor muscle, but inactive toward the adenosine deaminase fraction purified from the scallop mid-gut gland.