Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0021345 (infectious mononucleosis)
 3,358 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The heterophile antigen (Paul-Bunnell antigen, PBA) of infectious mononucleosis was isolated by extraction of an aqueous suspension of bovine erythrocyte stromata with chloroform-methanol (2:1). The upper aqueous layer contained gangliosides, PBA, and a high-molecular-weight glycoprotein. PBA and gangliosides were separated from the high-molecular-weight glycoprotein by extraction of lyophilized upper layer with chloroform-methanol solvents. Separation of PBA from gangliosides was carried out by chromatography on DEAE-cellulose with chloroform-methanol solvents. PBA appeared to be a minor glycoprotein component of the erythrocyte membrane and had both hydrophobic and hydrophilic properties. It was soluble in either organic or aqueous solvents. On SDS-polyacrylamide gel electrophoresis, it migrated as a single component that stained for protein with Coomassie blue, for carbohydrate with periodic acid-Schiff reagent, and for lipid with oil red 0; it had an apparent molecular weight of 26,000. It was composed of 62% protein with major amino acids; glutamic acid, proline, glycine, isoleucine, leucine, and threonine (158, 116, 98, 90, 85, and 82 residues per 1,000 residues, respectively). Carbohydrate content was 9.2% with major sugar constituents: sialic acid, galactosamine, and galactose. Serologic activity of PBA was destroyed by pronase but not by trypsin.
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PMID:Isolation and partial characterization of the heterophile antigen of infectious mononucleosis from bovine erythrocytes. 40 89

A glycoprotein was isolated from goat erythrocyte membranes by extraction with hot 75% ethanol. The glycoprotein was purified by ethanol precipitation, phosphocellulose chromatography gel filtration, ethyl:ether and chloroform:methanol extraction. In aqueous phosphate-buffered saline, pH 7, the glycoprotein was in an aggregated state with a sedimentation coefficient (S(obs)) to 1.5. Electrophoresis of the glycoprotein on polyacrylamide gels containing phosphate-buffered 0.1% SDS gave a single band, staining with both periodic acid Schiff (PAS) and Coomassie Blue (CB). The apparent m.w., calculated from retardation coefficient, was 25,000. Electrophoresis of the glycoprotein on 1% SDS gels buffered with Tris-acetate (pH 7.4) showed a major band of similar (23,500) apparent m.w. plus four other PAS- and CB-staining bands of lower mobility. With 131I-labeled glycoprotein, recovery of bands from gels, sialic acid analysis, heterophile antigen activity, and re-electrophoresis, it was shown that these additional bands were aggregated forms of a single or closely related glycoprotein species. The purified glycoprotein contained 50% carbohydrate with molar ratios of sialic acid:galactose:mannose:galactosamine:glucosamine of 3.1:2.1:0.1:1.6:1. The glycoprotein was highly reactive with the Paul-Bunnell heterophile antibody in the sera of patients with infectious mononucleosis, with Limulus polyphemus lectin and weakly ractive with wheat germ agglutinin. These reactivities were destroyed by neuraminidase treatment or by alkaline sodium borohydride. The native glycoprotein did not react with lectins from Canavalia enisformis, Phaseolus vulgaris, Ricinus communis, or Vicia graminea although it was reactive with the latter two after neuraminidase treatment.
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PMID:Immunochemical studies of infectious mononucleosis. V. Isolation and characterization of a glycoprotein from goat erythrocyte membranes. 95 50

Sera of 198 patients with infectious mononucleosis (IM), which were obtained during the 3rd or 4th week of the disease, were studied for the presence of antibodies to BS and B antigens of the Paul--Bunnell (P-B) antigenic complex. Six of these IM patients had anti-B antibodies without or with very low-titer anti-BS antibodies and the remaining patients had both types of antibodies at high titers. These 6 IM patients would have been misdiagnosed as seronegative if the traditional P-B tests with sheep erythrocytes had been employed. BS antigen was demonstrated in a large amount in chloroform-methanol extracts of peripheral blood buffy coat and of erythrocytes obtained from 1 of the 6 patients during the 3rd week of the disease and right after recovery.
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PMID:Studies on Paul--Bunnell (P-B) antigen--antibody system. IV. Unresponsiveness to one of P-B antigens in infectious mononucleosis. 640 83

The BS antigen, the component of the Paul-Bunnell (P-B) antigen complex that is shared by bovine (BRBC) and sheep red blood cells (SRBC), was demonstrated in chloroform-methanol extracts from peripheral blood leukocytes of 4 of 26 healthy young individuals. One of the extracts formed a precipitation line with infectious mononucleosis (IM) sera, which merged into a reaction of identity with the corresponding line formed by the purified P-B antigen of BRBC. The BS antigen of the P-B complex was also demonstrated in tissue sediments of an apparently normal human kidney by means of mixed agglutination test with IM sera and trypsinized BRBC as the indicator. Results of this study suggest that the BS antigen is expressed in normal tissues of some individuals as an intracellular antigen, whereas in various pathologic conditions it is expressed as cell-surface antigen and/or appears in a soluble form in the patient's circulation.
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PMID:Paul-Bunnell antigen in normal human tissues. 643 29

Preparations obtained by the chloroform-methanol extraction procedure from spleen tissues of patients with Hodgkin's disease, lymphomas, and leukemias, as well as from peripheral blood buffy coat of infectious mononucleosis (IM) patients were studied for the presence of 2 Paul-Bunnell (P-B) antigens; BS antigen shared by bovine red blood cells (BRBC) and sheep red blood cells (SRBC) and another, B antigen characteristic for BRBC. Both BS and B antigens were demonstrated by means of agglutination inhibition tests in over 40% of these extracts. None of the extracts from spleens, tonsils, and buffy coat of apparently normal human beings contained these antigens. P-B antigens of lymphoma-leukemia extracts were further purified by DEAE-Sephadex column chromatography. The purified fractions of some of these spleen extracts formed a precipitation line with IM sera, which merged into a reaction of identity with the lines formed by P-B antigens of BRBC. In studying various pathologic sera, B antigen was detected in sera of 28% of lymphoma-leukemia patients, 15% of patients with carcinomas of internal organs, and 3% of patients with systemic lupus erythematosus. On the other hand, BS antigen was found in only 3% of lymphoma-leukemia sera. These results confirmed our previous observations and indicated that both BS and B antigens are expressed as neoantigens on the patient's spleen cells as a result of pathologic processes in lymphoreticular malignancies.
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PMID:Studies on Paul-Bunnell (P-B) antigen-antibody system. II. P-B antigens in extracts of lymphoma-leukemia spleens and pathologic sera. 697 12