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ELECTROPHORETIC AND IMMUNOLOGICAL ANALYSES OF SEVEN CHLOROSARCINACEAN ALGAE 1
Author(s) -
Thomas Dempsey L.,
Groover Robert D.
Publication year - 1973
Publication title -
journal of phycology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.85
H-Index - 127
eISSN - 1529-8817
pISSN - 0022-3646
DOI - 10.1111/j.1529-8817.1973.tb04095.x
Subject(s) - biology , malate dehydrogenase , peroxidase , biochemistry , leucine , red algae , algae , aminopeptidase , isozyme , serology , genus , botany , enzyme , amino acid , genetics , antibody
SUMMARY 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.