Premium
Autolytic Enzyme System of Clostridium botulinum
Author(s) -
Takumi Kenji,
Kawata Tomio,
Hisatsune Kazuhito
Publication year - 1971
Publication title -
japanese journal of microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.664
H-Index - 70
eISSN - 1348-0421
pISSN - 0021-5139
DOI - 10.1111/j.1348-0421.1971.tb00562.x
Subject(s) - autolysin , chemistry , biochemistry , clostridium botulinum , amidase , cell wall , enzyme , peptidoglycan , alanine , amino acid , toxin
The mode of action of the autolytic enzymes of Clostridium botulinum type A strain 190L was investigated using a partially purified autolysin. The autolysin completely solubilized SDS‐treated cell walls of the organism, liberating 1.2 moles of NH 2 ‐terminal‐L‐alanine and 0.6 moles of reducing groups per mole of glutamic acid. Neither the NH 2 ‐termini of other amino acids nor COOH‐termini of any amino acids were released. These results show that the autolysin contains an N ‐acetylmuramyl‐L‐alanine amidase and a hexosaminidase. A disaccharide and peptides were isolated from the wall lysate in a chromatographically homogeneous state. The reducing end of the disaccharide was elucidated to be N ‐acetylglucosamine by borohydride reduction. This fact indicates that the hexosaminidase is likely to be an endo‐β‐ N ‐acetylglucosaminidase. A possible structure of the cell wall peptidoglycan is proposed.