Immunochemical studies on the poly-γ-D-glutamyl capsule of Bacillus anthracis. I. Characterization of the polypeptide and of the specificity of its reaction with rabbit …
JW Goodman, DE Nitecki - Biochemistry, 1966 - ACS Publications
JW Goodman, DE Nitecki
Biochemistry, 1966•ACS PublicationsCapsular polypeptide from a strain of Bacillus anthracis was isolated and found to consist
almost exclusively of D-glutamic acid with possible traces of aspartic acid; hexose content,
as determined by reactionwith orcinol, was negligible. The molecular weight of the
polypeptide, as estimated by terminal amino end group analysis using
trinitrobenzenesulfonic acid, was 33,500±3800. Antisera which precipitated with the purified
polypeptide were elicited in rabbits by repeated injections of suspensions of encapsulated …
almost exclusively of D-glutamic acid with possible traces of aspartic acid; hexose content,
as determined by reactionwith orcinol, was negligible. The molecular weight of the
polypeptide, as estimated by terminal amino end group analysis using
trinitrobenzenesulfonic acid, was 33,500±3800. Antisera which precipitated with the purified
polypeptide were elicited in rabbits by repeated injections of suspensions of encapsulated …
Capsular polypeptide from a strain of Bacillus anthracis was isolated and found to consist almost exclusively of D-glutamic acid with possible traces of aspartic acid; hexose content, as determined by reactionwith orcinol, was negligible. The molecular weight of the polypeptide, as estimated by terminal amino end group analysis using trinitrobenzenesulfonic acid, was 33,500±3800. Antisera which precipitated with the purified polypeptide were elicited in rabbits by repeated injections of suspensions of encapsulated organisms.
ACS Publications