Document 0083
 DOCN  M9470083
 TI    Glycoforms of alpha 1-acid glycoprotein in sera of human
       immunodeficiency virus-infected persons.
 DT    9409
 AU    Mackiewicz A; Khan MA; Gorny A; Kapcinska M; Juszczyk J; Calabrese LH;
       Espinosa LR; Department of Cancer Immunology, Academy of Medicine,
       GreatPoland; Cancer Center, Poznan.
 SO    J Infect Dis. 1994 Jun;169(6):1360-3. Unique Identifier : AIDSLINE
       MED/94253601
 AB    In acute infections thus far studied, there is a relative increase in
       plasma protein glycoforms rich in biantennary complex type N-glycans
       (type I), while in some diseases with chronic inflammatory changes,
       there is increase in glycoforms with more branched N-glycans (type II).
       In sera of 109 human immunodeficiency virus (HIV)-infected persons, 38
       rheumatoid arthritis patients, and 44 healthy subjects, the composition
       of alpha 1-acid glycoprotein (AGP) glycoforms was studied using crossed
       immunoaffinity electrophoresis with concanavalin A as a ligand. In
       patients in CDC classifications I, II, and III, distribution of AGP
       glycoforms was analogous to that in normal subjects. Type I alterations
       were observed in patients in group IV who had no signs of arthritis.
       Type II changes, analogous to those found in rheumatoid arthritis, were
       seen in group IV patients who developed arthritis. Most significant type
       I changes were associated with Pneumocystis carinii pneumonia
       (specificity, 100%; sensitivity, 96%).
 DE    Arthritis/BLOOD/COMPLICATIONS  C-Reactive Protein/ANALYSIS
       Glycosylation  Human  HIV Infections/*BLOOD/COMPLICATIONS
       Orosomucoid/*ANALYSIS/CHEMISTRY  Support, Non-U.S. Gov't  JOURNAL
       ARTICLE

       SOURCE: National Library of Medicine.  NOTICE: This material may be
       protected by Copyright Law (Title 17, U.S.Code).