Immunological characterization of Escherichia coli B glycogen synthase and branching enzyme and comparison with enzymes from other bacteria

Abstract

Escherichia coli B glycogen synthase and branching enzyme, although similar in amino acid composition, had no significant immunological cross-reactivity. The N-terminal sequences of the glycogen synthase were rich in hydrophobic residues, whereas branching enzyme had a higher content of acidic and basic residues. However, residues 21 to 28 of glycogen synthase and 7 to 14 of branching enzyme shared six of eight residues in common. Two fractions of branching enzyme, branching enzymes I and II, which can be isolated from E. coli B cell extracts, have been shown to be immunologically identical, suggesting that only one type of branching enzyme activity is present in E. coli B. Evidence has been obtained which indicates that E. coli B glycogen synthase and branching enzyme are antigenically very similar to glycogen synthases and branching enzymes from other enteric bacteria. No cross-reactivity with either enzyme was observed in cell extracts from photosynthetic bacteria.