Document Detail


Characterization of acid phosphatase activities in the equine pathogen Streptococcus equi.
MedLine Citation:
PMID:  11108009     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Acid phosphatases hydrolyse phosphomonoesters at acidic pH in a variety of physiological contexts. The recently defined class C family of acid phosphatases includes the 32 kDa LppC lipoprotein of Streptococcus equisimilis. To define further the distribution of acid phosphatases in the genus Streptococcus we have examined the equine pathogens Streptococcus equi subsp. equi and Streptococcus equi subsp. zooepidemicus. Whole cell assays indicated that these organisms possess two acid phosphatases with activity optima at pH 5.0 and pH 6.0-6.5 and that only the former of these was, like LppC, resistant to EDTA. Western blotting with a polyclonal anti-LppC antiserum revealed the presence of a cross-reactive 32 kDa protein in both organisms. The cross-reactive protein in S. equi was shown to be a surface accessible lipoprotein as its processing was inhibited by the antibiotic globomycin and it was released from whole cells by treatment with trypsin. The presence of DNA sequences homologous to the S. equisimilis lppC gene were confirmed by PCR. These data strongly suggest that Streptococcus equi subsp. equi and Streptococcus equi subsp. zooepidemicus produce a lipoprotein acid phosphatase homologous to LppC of S. equisimilis.
Authors:
A Hamilton; D Harrington; I C Sutcliffe
Related Documents :
932249 - Ultrastructural localization of acid phosphatase in normal and x-irradiated epidermis.
2474259 - Visualization of acid phosphatase activity on nitrocellulose filters following electrob...
10884579 - Kinetics of hydrolysis of dextran-methylprednisolone succinate, a macromolecular prodru...
16917129 - Phosphatidic acid osmotically destabilizes lysosomes through increased permeability to ...
14326109 - Cytochemical localization of acid phosphatases in euglena gracilis.
337889 - Measurement of phosphatases in biological fluids.
3355159 - Micellization of fatty acyl-coa mixtures and its relevance to the fatty acyl selectivit...
1817039 - Sialic acid storage disorders: observations on clinical and biochemical variation.
24118589 - Ampa receptor subunits expression and phosphorylation in cingulate cortex in rats follo...
Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Systematic and applied microbiology     Volume:  23     ISSN:  0723-2020     ISO Abbreviation:  Syst. Appl. Microbiol.     Publication Date:  2000 Oct 
Date Detail:
Created Date:  2001-02-28     Completed Date:  2001-03-22     Revised Date:  2003-11-14    
Medline Journal Info:
Nlm Unique ID:  8306133     Medline TA:  Syst Appl Microbiol     Country:  GERMANY    
Other Details:
Languages:  eng     Pagination:  325-9     Citation Subset:  IM    
Affiliation:
School of Sciences, University of Sunderland, UK.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Acid Phosphatase / isolation & purification*
Animals
Blotting, Western
Horse Diseases / microbiology
Horses
Hydrogen-Ion Concentration
Lipoproteins / genetics,  isolation & purification*
Polymerase Chain Reaction
Streptococcus equi / enzymology*,  pathogenicity
Chemical
Reg. No./Substance:
0/Lipoproteins; EC 3.1.3.2/Acid Phosphatase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  Comparative analysis of the whole set of rRNA operons between an enterohemorrhagic Escherichia coli ...
Next Document:  Identification of methionine-processed HPr in the equine pathogen Streptococcus equi.