Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5208
pubmed:dateCreated
1995-5-12
pubmed:abstractText
African trypanosomes cause disease in humans and animals. Trypanosoma brucei brucei affects cattle but not humans because of its sensitivity to a subclass of human high density lipoproteins (HDLs) called trypanosome lytic factor (TLF). TLF contains two apolipoproteins that are sufficient to cause lysis of T. b. brucei in vitro. These proteins were identified as the human haptoglobin-related protein and paraoxonase-arylesterase. An antibody to haptoglobin inhibited TLF activity. TLF was shown to exhibit peroxidase activity and to be inhibited by catalase. These results suggest that TLF kills trypanosomes by oxidative damage initiated by its peroxidase activity.
pubmed:grant
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Neoplasm, http://linkedlifedata.com/resource/pubmed/chemical/Aryldialkylphosphatase, http://linkedlifedata.com/resource/pubmed/chemical/Blood Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Carboxylic Ester Hydrolases, http://linkedlifedata.com/resource/pubmed/chemical/Catalase, http://linkedlifedata.com/resource/pubmed/chemical/Esterases, http://linkedlifedata.com/resource/pubmed/chemical/HPR protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Haptoglobins, http://linkedlifedata.com/resource/pubmed/chemical/Hemoglobins, http://linkedlifedata.com/resource/pubmed/chemical/Lipoproteins, LDL, http://linkedlifedata.com/resource/pubmed/chemical/Peroxidases, http://linkedlifedata.com/resource/pubmed/chemical/arylesterase
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0036-8075
pubmed:author
pubmed:issnType
Print
pubmed:day
14
pubmed:volume
268
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
284-6
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:7716520-Amino Acid Sequence, pubmed-meshheading:7716520-Animals, pubmed-meshheading:7716520-Antigens, Neoplasm, pubmed-meshheading:7716520-Aryldialkylphosphatase, pubmed-meshheading:7716520-Blood Proteins, pubmed-meshheading:7716520-Carboxylic Ester Hydrolases, pubmed-meshheading:7716520-Catalase, pubmed-meshheading:7716520-Endocytosis, pubmed-meshheading:7716520-Esterases, pubmed-meshheading:7716520-Haptoglobins, pubmed-meshheading:7716520-Hemoglobins, pubmed-meshheading:7716520-Humans, pubmed-meshheading:7716520-Hydrogen-Ion Concentration, pubmed-meshheading:7716520-Intracellular Membranes, pubmed-meshheading:7716520-Lipid Peroxidation, pubmed-meshheading:7716520-Lipoproteins, LDL, pubmed-meshheading:7716520-Lysosomes, pubmed-meshheading:7716520-Molecular Sequence Data, pubmed-meshheading:7716520-Oxidation-Reduction, pubmed-meshheading:7716520-Peroxidases, pubmed-meshheading:7716520-Trypanosoma brucei brucei
pubmed:year
1995
pubmed:articleTitle
Killing of trypanosomes by the human haptoglobin-related protein.
pubmed:affiliation
Department of Biochemistry and Molecular Genetics, School of Medicine and Dentistry, University of Alabama at Birmingham 35294, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't