Forskning
Udskriv Udskriv
Switch language
Region Hovedstaden - en del af Københavns Universitetshospital
Udgivet

Purification and characterization of a major human Pneumocystis carinii surface antigen

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

DOI

  1. Leukemogenic nucleophosmin mutation disrupts the transcription factor hub regulating granulo-monocytic fates

    Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

  2. Hypoglycemia unawareness in type 1 diabetes suppresses brain responses to hypoglycemia

    Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

  3. Breaking down brain barrier breaches in cerebral malaria

    Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

  4. A liver stress-endocrine nexus promotes metabolic integrity during dietary protein dilution

    Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

  5. Neutrophil extracellular traps - the dark side of neutrophils

    Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

  1. Profound Endothelial Damage Predicts Impending Organ Failure and Death in Sepsis

    Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

  2. The Danish Microbiology Database (MiBa) 2010 to 2013

    Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

Vis graf over relationer
Previous studies of Pneumocystis carinii have identified the major surface antigen of rat and human isolates as proteins of 116,000 and 95,000 mol wt, respectively, that are antigenically not identical. In this study both rat and human P. carinii proteins were purified by solubilization with zymolyase followed by molecular sieve and ion exchange chromatography. The native proteins had an apparent mol wt of 290,000 or greater, based on molecular sieve studies as well as cross-linking studies. Both proteins were glycoproteins; treatment with endoglycosidase H resulted in a 9% decrease in mol wt. The carbohydrate composition of the rat P. carinii glycoprotein was distinct from the human isolate; glucose, mannose, galactose, and glucosamine occurred in approximately equimolar ratios in the human P. carinii protein, whereas glucose and mannose were the predominant sugars of the rat P. carinii protein. To evaluate humoral immune responses to the human P. carinii protein, an enzyme-linked immunosorbent assay using purified protein was developed. Some, but not all, patients who subsequently developed P. carinii pneumonia demonstrated a serum antibody response to the surface antigen. Nearly all subjects without a history of P. carinii pneumonia had no detectable antibodies. Purified P. carinii proteins will greatly facilitate the investigation of host-P. carinii interactions.
OriginalsprogEngelsk
TidsskriftJournal of Clinical Investigation
Vol/bind87
Udgave nummer1
Sider (fra-til)163-70
Antal sider8
ISSN0021-9738
DOI
StatusUdgivet - jan. 1991

ID: 39874166