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Biomedical subjects

B Sabo

Publications and source records attributed to B Sabo.

At least 19 recordsLinked to original sources
PubMed2001

Environmental sensitivities: prevalence of major symptoms in a referral center: the Nova Scotia Environmental Sensitivities Research Center Study.

Although the phenomenon of environmental sensitivities (ES) has no clear etiology nor well-accepted pathophysiology, affected individuals experience symptoms that cause varying levels of dysfunction. Through a dedicated, government-funded research and treatment center, a detailed questionnaire covering 217 symptoms in 13 systems was mailed in 1997-1998 to 812 individuals referred to the center by physicians. A total of 385 (47%) questionnaires were returned, and data were analyzed on 351 individuals. Participants tended to be women (80%), middle-aged individuals (37% age 40-49 years), and those in higher educational groups (28% completed university), but there was wide variation in demographic variables. General symptoms such as difficulty concentrating, fatigue, forgetfulness, and irritability dominated the overall prevalence of symptoms since the start of their illness. Those related to irritation such as sneezing, itchy or burning eyes, and hoarseness or loss of voice were more common after exposure to environmental irritants. Ranking of symptoms using severity scores was consistent between men and women. Overall scores were higher in women, in participants who were separated or divorced, and in low-income groups. The type and consistency of symptoms experienced after exposure to triggering substances may not fit a purely psychogenic theory.

Adolescent↗
PubMed1999

Anesthetic considerations in patients undergoing percutaneous radiofrequency interstitial tissue ablation.

Radiofrequency (RF) interstitial tissue ablation is a new, minimally invasive procedure for patients with liver cancer who are not candidates for conventional therapy. The percutaneous RF ablation therapy involves placing a needle electrode under ultrasound guidance into a selected portion of the tumor and heating the tissue between 90 degrees C and 100 degrees C. The ablation procedure can be done under monitored anesthesia care on an outpatient basis. The patient's ability to cooperate with regard to breathing is critical for accurate needle placement. Intravenous sedation must be meticulously titrated to maintain a delicate balance of patient cooperation and optimal comfort.

Anesthesia↗
PubMed1989

Survival of infants with persistent pulmonary hypertension without extracorporeal membrane oxygenation.

A retrospective evaluation was performed of the survival after conservative therapy of infants with persistent pulmonary hypertension who met the published criteria of Bartlett et al (Pediatrics. 1985;76:479-487) or Short et al (Clinics in Perinatology. 1987;14:737-748) for extracorporeal membrane oxygenation (ECMO) therapy. An 80% to 90% mortality rate can be predicted with these criteria, which are based on historical data, if ECMO is not used. The records of infants with the diagnosis of persistent pulmonary hypertension, weighing greater than 2 kg at birth and who were treated during two time periods, January 1980 to December 1981 [23 patients] and January 1986 to December 1988 [17 patients], were reviewed. During the earlier period, hyperventilation was the mainstay of our therapy, whereas during the later period, a more conservative approach (avoidance of hyperventilation) was adopted. In 1980 to 1981, 1 of the 6 patients (17%) who were eligible for ECMO by criteria of Bartlett et al survived, which is consistent with the published data. However, in 1986 to 1988, 9 of 10 ECMO-eligible patients (90%) survived (P less than .02). The corresponding survival figures using the alveolar-arterial oxygen difference criteria of Short et al were 0 of 5 survivors (0%) in 1980 to 1981 and 8 of 9 (89%) in 1986 to 1988 (P less than .006). These data indicate that approximately 90% of patients who are candidates for ECMO now survive in our institution without the use of that therapy.(ABSTRACT TRUNCATED AT 250 WORDS)

Birth Weight↗
PubMed1988

Evaluation of rebreathing in patients undergoing cataract surgery.

Ten patients undergoing elective cataract surgery with local anesthesia were evaluated for rebreathing using mass spectrometry and arterial blood gas analysis. Results showed a 10 or 51 oxygen-air mixture with an inspired oxygen concentration of 50% (FIO2) administered via a face tent maintained normal blood gases and a satisfactorily low inspired carbon dioxide (FICO2) in conscious patients who were free of lung disease.

Adult↗
PubMed1986

Membrane glycophorins in Sta blood group erythrocytes.

Structural and immunochemical studies of glycophorins isolated from erythrocytes of an individual homozygous for the M Sta blood group phenotype are described. Reactivities with specific monoclonal antibodies indicated that two major M and N glycophorins were present. The M and N Sta glycophorins were resolved by Lens culinaris lectin affinity chromatography. The N species was not held on the lectin but the M species, like control alpha glycophorins, was retained and could be eluted with alpha-methylmannoside. The two proteins were present in almost equimolar amounts. Studies of the CNBr fragments provided evidence that the structure of M Sta glycophorin is the same as that of the usual M alpha glycophorin but that the N Sta glycophorin is a variant. The amino-terminal octapeptides of the M and N species were similar in amino acid and carbohydrate composition to those isolated, respectively, from M and N alpha glycophorins. The studies focused on CNBr glycopeptide B that, in control alpha glycophorins, extends from amino acid residues 9 to 81. The fragment from the M species exhibited properties identical to those of the corresponding fragment of control alpha glycophorins in terms of size, chromatographic behavior, amino acid and carbohydrate contents and compositions, the presence of O-glycosidically linked saccharides and a single Asn-linked carbohydrate unit. The structures of the O-linked units were inferred experimentally to be NeuAc(alpha 2,3)Gal-(beta 1,3)GalNAc and NeuAc(alpha 2,3)Gal(beta 1,3) [NeuAc(alpha 2,6)]GalNAc, present in a ratio similar to that found in controls; and the Asn-linked unit also appeared to be as in the control. The tryptic glycopeptide pattern of the M Sta glycophorin CNBr fragment B was identical to the pattern of the corresponding control fragment, and the composition of the tryptic peptides suggested sequence identity with the control fragment. In contrast, the N Sta glycophorin yielded two CNBr glycopeptides B; both contained fewer amino acid residues and virtually lacked Man and GlcNAc, indicating the absence of the Asn-linked carbohydrate. The much decreased levels of these carbohydrates in the intact N protein, corroborated the latter finding. The O-glycosidic saccharides appeared similar to those found in control alpha glycophorins. However, the tryptic glycopeptide pattern of the variant differed from control M or N alpha glycophorins, suggesting a deletion of a large segment of the molecule near residues 40-61 and/or a substitution of methionine for a residue upstream from residue 40.(ABSTRACT TRUNCATED AT 400 WORDS)

Amino Acids↗
PubMed1983

A carbohydrate structural variant of MM glycoprotein (glycophorin A).

A variant of the MM glycoprotein (glycophorin A) was isolated from erythrocyte membranes of two individual donors, a mother (L.G.) and daughter (V.W.). This glycoprotein was found to be a carbohydrate variant in which, for both donors, certain O-glycosidically linked saccharides retained the core structure consisting of NeuAc(alpha 2,3)Gal(beta 1,3)GalNAc that is common to all O-linked saccharides of the MN glycoproteins, and, in addition, contained substituents, of varying chain lengths, on the primary carbinol of GalNAc. These saccharides were released from the polypeptide by beta-elimination in the presence of sodium borohydride, and aspects of their structure were investigated by glycosidase digestion and periodate oxidation. Thus, the smallest variant structure was deduced to be NeuAc(alpha 2,3)Gal(beta 1,3)[GlcNAc(beta 1,6)]H2GalNAc. The 6-O-linked GlcNAc appears to serve as the focus of further chain elongation reactions, involving alternate additions of Gal and GlcNAc residues and leading to the formation of several homologous structures. Two such structures, NeuAc(alpha 2,3)Gal(beta 1,3)[GlcNAc(beta 1,?) Gal(beta 1,3/4)GlcNAc(beta 1,6)]H2GalNAc and NeuAc(alpha 2,3) Gal(beta 1,3)[Gal(beta 1,3/4)GlcNAc(beta 1,6)]H2GalNAc were the predominant species present. A larger saccharide was also isolated and its partial sequence was determined to be Gal(beta 1,3/4)GlcNAc(beta 1,?)[Gal(beta 1,3/4)Glc-NAc(beta 1,?)] Gal(beta 1,3/4)GlcNAc(beta 1,6)[NeuAc(alpha 2,3)Gal-(beta 1,3)]H2GalNAc. Because the peptide portion of these glycoproteins contains two methionine residues, it was possible to isolate two CNBr glycopeptides from separate regions of the molecule, and to assess the distribution of these variant structures in the polypeptide. The saccharides were linked to about 2-3 Ser and/or Thr residues in the donor LG glycoprotein and one of the attachment sites was located within the CNBr glycooctapeptide representing the NH2 terminus. Considerable heterogeneity in saccharide structure was documented for this site, and it is likely that such heterogeneity occurs also at other sites. The variant saccharides bear structural similarities to the core region of O-linked saccharides of certain blood group-active mucins and ovarian cyst secretions, and to the outer sequences of N-linked carbohydrate units (I-, i-active) of the major glycoprotein of human erythrocytes, band 3. The structures of the variant saccharides suggest that they may be potential precursors of H blood group-active carbohydrates, present in varying degrees of maturity, and attached to an integral protein of erythrocytes.

Carbohydrate Conformation↗
PubMed1982

Bgb expression in relation to the HLA-B17 antigen splits Bw57 and Bw58 and the cross-reactions of anti-Bgb antibodies.

A substantial number of individuals typed as HLA-B17 do not have Bgb. To determine whether or not this discrepancy reflects genetic or ethnic group differences or the influence of B17 antigen subtypes, a large number of unrelated and related B17 individuals from the Caucasian, Hispanic, Black and Chinese ethnic groups were tested in parallel for Bgb and Bw57- or Bw58- B17 subtype. Higher Bgb expression was found in association with Bw57, but differences in expression of Bgb were also seen in different ethnic groups and in different related individuals carrying the same Bw57 or Bw58 haplotype. Genetic factors other than HLA thus influence the expression of HLa Antigens on red cells. Standard and antiglobulin lymphocytotoxicity tests indicate that all Bgb typing sera contain anti-Bw57 antilymphocyte antibodies and most also contain anti-Bw58 and cross-reacting anti-B12, B15 and/or Bw49 antibodies.

Alleles↗
PubMed1982

Anti-Dp is anti-K14.

Explore the source record for details and available documents.

Antibody Specificity↗
PubMed1981

Erythrocyte glycosphingolipids of four siblings with the rare blood group p phenotype and their parents.

Erythrocytes that exhibit the rare blood group p phenotype lack the P antigen (globotetraosylceramide) and the Pk antigen (globotriaosylceramide). This phenotype is inherited as an autosomal recessive condition and the red cells of heterozygous individuals, parents and children of p persons, are serologically normal but no chemical analyses of their red cells have been reported. We have studied an unusual family in which all five children exhibit the p phenotype. In addition to the abnormalities described previously, the erythrocytes of four siblings had twice the normal concentration of lactotriaoslyceramide and lactoeotetraosylceramide. These cells also contained 3-5 times as much sialosyllactoneotetraosylceramide and up to a two-fold increase in Gm3 ganglioside. The glycolipids of the parents'erythrocytes were normal. Electrophoretic analysis of the glycoproteins of the proposita's erythrocytes revealed no abnormalities, but her erythrocyte membranes contained approximately 35% less galactosamine than normal red cells. This abnormality resulted from a marked decrease in galactosamine that was soluble in chloroformmethanol. The lipid-extracted residue, which contained the glycoproteins, had a normal galactosamine content.

Blood Group Antigens↗
PubMed1979

Another Kell-related antibody, anti-K19.

A new high-frequency antigen related to the Kell system was defined by the serum of a patient, Mrs. Sub. The antigen was lacking from her cells and those of one of her three siblings. All random cells tested were incompatible with her serum as were bloods of other various "null" phenotypes, but Ko bloods were compatible suggesting that the antibody, subsequently called anti-K19, was related to the Kell blood group system.

Absorption↗