Physico-chemical and immunological properties of allophycocyanins

Abstract

Allophycocyanins were purified from diverse cyanobacteria and one rhodophytan alga (Cyanidium caldarium). The native proteins are trimeric molecules with the structure (αβ)₃. Representative native allophycocyanins and their α and β subunits were characterized with respect to molecular weight, amino acid composition, isoelectric point, absorption and fluorescence spectra and immunological properties. All of the allophycocyanins studied were strikingly similar with respect to each of these properties. Renatured α and β subunits of allophycocyanin were distinct immunologically from each other, and both cross-reacted with the antiserum to the native protein. Trimeric allophycocyanin was readily reconstituted from the purified α and β subunits. Formation of hybrid allophycocyanins was demonstrated by direct isolation and characterization of the hybrid proteins and by immunological techniques. The results support the view that allophycocyanins are a highly conserved group of proteins.