title: Purification and specificity of bacteriolytic enzyme I from Hartmannella glebae.
abstract: A soil amoeba (Hartmannella glebae), when grown in conjunction with Enterobacter aerogenes and Alcaligenes faecalis, produced two enzymes. Enzyme I was purified by gel filtration on Sephadex G-100 and chromatography on diethylaminoethyl-cellulose. It is a basic protein. The analysis of the enzymic digest of the cell walls of Micrococcus lysodeikticus after reduction and acid hydrolysis showed that the enzyme cleaved the glycosidic bond between acetylmuramic acid and acetylglucosamine of the peptidoglycan moiety of the cell walls. The enzyme is identified as endo-beta-N-acetylmuramidase.
mesh_terms: D000421:Alcaligenes; D001433:Bacteriolysis; D002473:Cell Wall / Q000378:metabolism; D002729:Chloromercuribenzoates / Q000494:pharmacology; D004492:Edetic Acid / Q000494:pharmacology; D004754:Enterobacter; D006249:Hartmannella / Q000201:enzymology*; D008623:Mercaptoethanol / Q000494:pharmacology; D008837:Micrococcus / Q000648:ultrastructure; D009113:Muramidase / Q000302:isolation & purification* / Q000378:metabolism
chemical_list: D002729:Chloromercuribenzoates; D008623:Mercaptoethanol; D004492:Edetic Acid; D009113:Muramidase