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PMID: 192712 Published · ppublish English Journal Article

Resolution and purification of three periplasmic phosphatases of Salmonella typhimurium.

Journal of bacteriology ·Vol. 130 ·No. 1 ·1977-04-00 ·Pages 399-410

Kier LD, Weppelman R, Ames BN

Abstract

A survey of Salmonella typhimurium enzymes possessing phosphatase or phosphodiesterase activity was made using several different growth conditions. These studies revealed the presence of three major enzymes, all of which were subsequently purified: a cyclic 2' ,3'-nucleotide phosphodiesterase (EC 3.1.4.d), an acid hexose phosphatase (EC 3.1.3.2), and a nonspecific acid phosphatase (EC 3.1.3.2). A fourth enzyme hydrolyzed bis-(p-nitrophenyl)phosphate but none of the other substrates tested. No evidence was found for the existence of an alkaline phosphatase (EC 3.1.3.1) or a specific 5'-nucleotidase (EC 3.1.3.5) in S. typhimurium LT2. All three phosphatases could be measured efficiently in intact cells, which suggested a periplasmic location; however, they were not readily released by osmotic shock procedures. The nonspecific acid phosphatase, which was purified to apparent homogeneity, yielded a single polypeptide band on both sodium dodecyl sulfate and acidic urea gel electrophoretic systems.

MeSH Terms
2',3'-Cyclic-Nucleotide Phosphodiesterases/analysis,isolation & purification,metabolism Acid Phosphatase/analysis,isolation & purification,metabolism Cell Membrane/enzymology Chromatography Electrophoresis, Polyacrylamide Gel Hexoses Phosphoric Diester Hydrolases/metabolism Salmonella typhimurium/enzymology
Chemicals
Hexoses Acid Phosphatase 2',3'-Cyclic-Nucleotide Phosphodiesterases Phosphoric Diester Hydrolases
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Kier L D
Weppelman R
Ames B N
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31 references, click to expand
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Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
DOI
10.1128/jb.130.1.399-410.1977
Published
1977-04-00
Pages
399-410
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC235218
Subset
IM
External Links
PubMed source DOI: 10.1128/jb.130.1.399-410.1977 PMC Full Text View journal details
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