| Abstract: | Proteins from 7 species of chlorosarcinacean algae representing 4 genera were studied with starch and disc gel electrophoresis and immunology to determine biochemical relationships. Migration patterns of enzymes and serological reactions indicated that 4 species of Chlorosarcinopsis were closely related, whereas Friedmannia israeliensis, Fasciculochloris boldii, and Chlorosarcina longispinosa were more diverse. Malate dehydrogenase, glutamate dehydrogenase, nonspecific alpha esterases, and peroxidase (using pyrogallol as the hydrogen donor) were present in all 7 species. No peroxidase activity occurred with benzidine. Leucine aminopeptidase was obvious in only 2 species. A single distinct band of general protein in F. israeliensis and C. longispinosa suggested the presence of homogenous reserve protein. The 7 species exhibited serological affinity to 4 isolates of Protosiphon representing diverse morphology within the genus. The data are discussed relative to current knowledge of comparative morphology of chlorosarcinacean algae. |
