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THE ORIGIN OF THE MULTIPLE FORMS OF PHOSPHORYLASE IN ALGAE *
Author(s) -
Fredrick Jerome F.
Publication year - 1964
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1111/j.1749-6632.1964.tb14231.x
Subject(s) - isozyme , glycogen phosphorylase , biochemistry , enzyme , algae , cofactor , adenosine , chemistry , biology , botany
Summary Two isozymes of phosphorylase are present in the alga Oscillatoria princeps that are similar to the animal phosphorylases in their need for adenosine‐5‐phosphate as cofactor. The biosynthesis of the adenosine‐5‐phosphate independent isozyme can be effectively blocked by the addition of the phytotoxic compound, 3‐amino‐1,2,4‐triazole, to cultures of the alga. Evidence is presented for the possible existence of a kinaselike enzyme that converts the AMP‐requiring isozyme in this alga to the AMP‐independent form. The evolutionary significance of these observations is examined.