[CITATION][C] Teichoic acid phosphorylcholine esterase: a novel enzyme activity in pneumococcus
JV Höltje, A Tomasz - Journal of Biological Chemistry, 1974 - Elsevier
JV Höltje, A Tomasz
Journal of Biological Chemistry, 1974•ElsevierA mutant of pneumococcus which lacks most of the usual autolysin (N-acetylmuramyl-l-
alanine amidase), contains another enzyme that can remove a maximum of 15 to 20% of
phosphorylcholine residues from pneumococcal cell walls and from the Forssman antigen.
An identical enzymatic activity was found to be also present in the wild type of
pneumococcus.
alanine amidase), contains another enzyme that can remove a maximum of 15 to 20% of
phosphorylcholine residues from pneumococcal cell walls and from the Forssman antigen.
An identical enzymatic activity was found to be also present in the wild type of
pneumococcus.
A mutant of pneumococcus which lacks most of the usual autolysin (N-acetylmuramyl-l-alanine amidase), contains another enzyme that can remove a maximum of 15 to 20% of phosphorylcholine residues from pneumococcal cell walls and from the Forssman antigen. An identical enzymatic activity was found to be also present in the wild type of pneumococcus.
Elsevier