Linked Life Data

2045782

Source:http://linkedlifedata.com/resource/pubmed/id/2045782

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1991-7-17
pubmed:abstractText
Helicobacter pylori is the major aetiological agent of gastroduodenitis in humans. Due to the potential importance of catalase in the growth and survival of Helicobacter pylori on the surface of inflamed mucosae, we have characterized catalase from H. pylori as a prelude to further studies on the function of the enzyme in vivo. The catalase activity of H. pylori was significantly affected by the presence of blood, serum or erythrocytes in the growth medium: the greatest activity was expressed when the bacterium was grown on medium containing serum. H. pylori catalase is a tetramer with a subunit Mr of 50,000. The enzyme had a pI of 9.0-9.3, was active over a broad pH range and was stable at 56 degrees C. It was non-competitively inhibited by sodium azide, and had no detectable peroxidase activity. The Km for the purified catalase was measured as 43 +/- 3 mM-H2O2 and the V as 60 +/- 3 mmol H2O2 min-1 (mg protein)-1. The native catalase has absorption maxima at 280 nm and 405 nm with further minor shoulders or peaks at 510 nm, 535 nm and 625 nm, consistent with the presence of an iron-porphyrin prosthetic group.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0022-1287
pubmed:author
pubmed:issnType
Print
pubmed:volume
137
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
57-61
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
Helicobacter pylori catalase.
pubmed:affiliation
School of Microbiology, University of New South Wales, Kensington, Australia.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't