Open AccessLocation of tyrosine phenol‐lyase in some Gram‐negative bacteria
Author(s) -
Nagasawa Toru,
Ishii Takafumi,
Yamada Hideaki
Publication year - 1985
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1985.tb01094.x
Subject(s) - tryptophanase , periplasmic space , biochemistry , lysozyme , spheroplast , biology , escherichia coli , enzyme , microbiology and biotechnology , chemistry , gene
Citrobacter intermedius, Escherichia coli and Proteus morganii were converted into spheroplasts by adding lysozyme and EDTA to the sucrose medium. The periplasmic enzymes alkaline phosphatase and 5′‐nucleotidase were released into the medium during spheroplasting, but the inducible tyrosine phenol‐lyase and tryptophanase remained in the spheroplasts, as did the cytoplasmic positional markers glutamate dehydrogenase and glucose‐6‐phosphate dehydrogenase, indicating that both enzymes are located in the cytoplasm.