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D-Ribulose 1,5-bisphosphate carboxylase was purified from the blue-green alga Anabaena cylindrica (Lemm) by procedures involving acid precipitation, ammonium sulfate fractionation, and Sephadex G-200 gel filtration. The enzyme was homogeneous by the criterion of polyacrylamide disc gel electrophoresis and was a multimer of a single-size polypeptide chain of 54,000 daltons. The carboxylases from four species of blue-green algae (Anabaena, Nostoc strain MAC, Agmenellum quadruplicatum strain PR-6, and Anacystis nidulans strain TX20) were closely similar in molecular size, since enzyme activity was eluted at the same volume after sucrose gradient centrifugation. Further analysis by gel filtration indicated that the four blue-green algal carboxylases were nearly identical in molecular weight, ranging from 449 to 453,000. The amino acid composition of the Anabaena carboxylase was determined and was found to resemble closely the composition of the large subunit from eukaryotic photosynthetic organisms.

Carbon dioxide assimilation in blue-green algae: initial studies on the structure of ribulose 1,5-bisphosphate carboxylase