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At least 19 recordsLinked to original sources
PubMed1976

Degradation of blood group antigens in human colon ecosystems. I. In vitro production of ABH blood group-degrading enzymes by enteric bacteria.

Human feces contain enzymes produced by enteric bacteria that degrade the A, B, and H blood group antigens of gut mucin glycoproteins. We have studied their production in fecal cultures to determine if such cultures can be a source for enzyme purification and to explore how blood group antigen-degrading enzymes are adapted in individual human colon ecosystems. They were present in fecal cultures from each of 27 healthy subjects, including ABH nonsecretors. Heat-sensitive obligate anaerobes are their major source. From 39 to 85% of the total enzyme activity produced by growing cultures was extracellular. Commercial hog gastric mucin and salivary glycoproteins, including Lea saliva which lacks A, B, and H antigens, enhance production of A-, B-, and H-degrading activity in anaerobic fecal cultures irrespective of the glycoprotein's blood group specificity. There is evidence that the host's ABO blood type and secretor status affects the specificity of blood group-degrading enzymes produced by his fecal bacteria in vitro. Thus, fecal inocula from B secretors incubated with hog gastric mucin (A and H specificity) or with Lea saliva produced greater levels of B-degrading than A- or H-degrading activity, and inocula from A secretors in similar media produced greater levels of A-degrading than B- or H-degrading activity. Blood group-degrading enzymes produced in fecal cultures are glycosidases and not proteases. The B-degrading enzyme cleaves the B antigenic determinant alpha-D-galactose from the oligosaccharide side chains of mucin glycoproteins with B specificity. Anaerobic fecal cultures containing blood group substances are a feasible source for purifying blood group antigen-degrading enzymes. Prior adaptation to blood group antigens in the gut mucins of type A and type B secretors affects the specificity of the enzymes produced in vitro.

ABO Blood-Group System↗
PubMed1976

[The biochemical aspects of blood group antigens].

The biochemical aspects of the immunodominant structures of blood groups antigens are mainly restricted to the following: ABH and Lewis in secretory fluids or on the red blood cells; P system (P1, P, Pk antigens); MN antigens and related; Tn and Tn antigens; Some hypothesis may be put forward for the I, i antigens. Many other antigens seem to be on the dependence of interactions between proteins and lipids of the red cell membrane; such immunodominant structures are not yet known. Except for the ABH and Lewis groups, the biosynthesis pathways are at present unclear.

ABO Blood-Group System↗
PubMed1979

Frequency of blood group antigens in Nigerian children with falciparum malaria.

The frequencies of the following blood group antigens: A, B, O, M, N, S, s, U, Fya, FyB, Lea, Jsa and K have been determined in Nigerian children with severe falciparum malaria. The frequency distribution of M, N, S, s, U, Fya and Fyb were not significantly different in children with life-threatening falciparum malaria and controls. The frequencies of A, B, O, Lea, Jsa and K found in the children with severe malaria were similar to those previously reported for healthy adults in this population. The Duffy blood group antigens Fya and Fyb were virtually absent from both infected and control children. This finding is in variance with a Fya frequency of 23% reported by Worlledge et al. (1974) for healthy adults in this population.

ABO Blood-Group System↗
PubMedDate not supplied

Hemagglutination inhibition studies for the evaluation of blood group antigens in ethanol soluble substances (ESS) obtained from human, baboon and vervet monkey red blood cells.

Soluble blood group substances, isolated from the red blood cells of humans, baboons, and vervet monkeys by ethanol extraction, possessed serologically active specificities for the following antigens: A, B, H, Lea, LebL, P, P19 Pk and I. Human red blood cells lacking any of these specificities by the direct hemagglutination test also lacked the related antigens in their soluble extract. The only exception was in "Bombay" Oh cells, from which soluble H substance could be readily isolated. Soluble substances obtained from baboon and vervet monkey red blood cells, which lack the human variety of A, B, and H antigens on their red blood cells, inhibited both human and lectin anti-H reagents. The detection of "hidden" H activity in Oh cells will pose some important questions regarding membrane characteristics and the role of immune surveilance.

ABO Blood-Group System↗
PubMed1979

Lack of blood group antigen A on human corneal endothelium.

Using direct immunofluorescence and mixed agglutination, we did not find blood group antigen A on human corneal endothelium from patients of blood type A or AB. The antigen was easily detected on the epithelium of these patients. We believe that the ABO blood group antigens are probably absent on human corneal endothelium, therefore they cannot play a direct role in specific corneal endothelial rejection.

ABO Blood-Group System↗
PubMed1978

Structural properties of the human MN blood group antigen receptor sites.

It is shown that the MN blood group antigen determinant of the major human erythrocyte membrane (MN) sialoglycoprotein is located on its N-terminal octaglycopeptide. The only analytically detectable difference between peptides from MM and NN cells are Ser/Leu and Gly/Glu polymorphisms at the first and fifth positions, respectively. Destruction of the antigens by removal of the N-terminal residues suggests that these amino acids represent a part of the receptor areas for various anti-M or -N reagents. Evidence is presented that the N-terminal structure of the Ss glycoprotein is identical with that of MN glycoprotein from NN red cells up to the fifth residue. This provides an explanation for the 'N' antigen on this molecule and direct support for the earlier proposal that the MNSs locus is represented by homologous genes.

Binding Sites, Antibody↗
PubMed1979

Doa (Dombrock) blood group antigen in the Japanese.

Blood samples from 100 unrelated Japanese were tested for Doa antigen. It was found that the frequency of the antigen in the Japanese (18%) is lower by far than in Caucasians, Negroes or American Indians.

Blood Group Antigens↗
PubMed1977

The relationship between expression of epithelial B-like blood group antigen, cell movement and cell proliferation.

Healing wounds in the oral mucosa of rhesus monkeys were examined by an immunofluorescence staining method to demonstrate the distribution of a blood group antigen cross reacting with human group B, and by labelling with tritiated thymidine to localize areas of cell proliferation. Within hours, blood group antigen reactivity was lost from epithelial cells adjacent to the wound margin. Reactivity was absent from the epithelial outgrowth into the wound, but returned with restoration of epithelial continuity. The zone of increased cell proliferation lay adjacent to, but outside of, the area of antigen loss. Antigen loss appeared to be associated with an area of increased cell movement, a finding of interest in relation to reports of antigen loss from epithelial tumors.

ABO Blood-Group System↗
PubMed1977

Selective depression of blood group antigens associated with hereditary ovalocytosis among melanesians.

Recessively inherited ovalocytosis in coastal Melanesians is associated with widespread, but selective, depression of blood group antigens in homozygotes, who comprise about 15% of these populations. It is suggested that a membrane anomaly exists, and that the series of depressed determinants all depend, for their full expression, upon the same membrane component(s), the proper synthesis of which is being genetically affected. Affected antigens would thus be associated by position and/or structure. Antigens subject to depression include IT, IF, LW,D,C,e,S,s,U,Kpb,JKa,JKb,Xga,Wrb,Scl and Ena, which are simultaneously affected when present on oval cells. Reactivity of A1,ID,i,P1,M,N,Lub,k,Fya,Coa, Vel and Gea appears to be within the normal range on depressed cells, as does sialic acid content. Indirect evidence suggests that Z (associated with S and s) is among the depressed series, while NA and Leb are not. High H variants, common among Melanesians, seem absent among depressed bloods, and when such variants were excluded, H, A and B did not appear subject to depression. The distribution pattern of ovalocytosis suggests that it may confer some selective advantage in the tropical coastal environment. The findings also have implications concerning population genetic work in New Guinea.

ABO Blood-Group System↗
PubMed1979

Turtle-dove ovomucoid, a glycoprotein proteinase inhibitor with P1-blood-group antigen activity.

Ovomucoid from the egg white of turtle-dove (Streptopelia risoria) was purified and shown to be a glycoprotein of mol. wt. 29 400, with valine as N-terminal residue. It is an inhibitor of both trypsin and chymotrypsin, but has a lower affinity for trypsin than has hen ovomucoid. Turtle-dove ovomucoid contains antigenic activity cross-reacting with the blood-group-P1 antigen of human erythrocytes. Hen ovomucoid has no detectable blood group-P1 activity. The carbohydrate composition of turtle-dove ovomucoid differs from hen ovomucoid in having substantially higher galactose content. The possible relationship between carbohydrate composition and antigenic activity is discussed.

Amino Acids↗
PubMed1975

[Demonstration of blood group antigens of ABO system in human teeth].

The absorption-elution method allows the determination of the blood group properties of the ABO-System from human teeth. The results of own investigations carried out on a larger number of specimens are reported. The significance of the determination of the blood group antigens in teeth for the forensic stomatology is emphasized.

ABO Blood-Group System↗
PubMed1976

Degradation of blood group antigens in human colon ecosystems. II. A gene interaction in man that affects the fecal population density of certain enteric bacteria.

The autosomal dominant ABH secretor gene together with the ABO blood type gene control the presence and specificity of A, B, and H blood group antigens in human gut mucin glycoproteins. Certain obligate anaerobes in feces produce extracellular antigen-specific glycoside structures. We estimated the populations of these bacteria in feces of 22 healthy subjects by determining the greatest dilution of feces that yielded A, B, or H blood group-degrading enzyme activity after 24 h incubation in anaerobic cultures. Comparatively small populations of fecal bacteria produce blood group-degrading enzymes; their estimated populations were 10(8) per g or less in 21 subjects. Fecal populations of B-degrading bacteria were stable over time, and their population density averaged 50,000-fold greater in blood group B secretros than in other subjects. We present evidence that the greater fecal populations of B-degrading bacteria in B secretors is due in part to a competitive nutritional advantage gained by their ability to enzymatically cleave the B antigenic determinant alpha-D-galactose from gut mucins of B secretors. Fecal populations of bacteria producing A and H antigen-degrading enzyme activities were comparable in all subjects to the fecal population of B-degrading bacteria in B secretors. The large populations of fecal anaerobes may be an additional source of A antigen substrate for A-degrading bacteria; thus, antigens cross-reacting with A antigen were detected on cell walls of anaerobic bacteria from 3 of 10 cultures inoculated with 10(-10) g feces. Bacteria producing B-degrading activity likely represent a separate population from those producing A- or H-degrading activity since their fecal populations differed numerically in 14 subjects. These findings suggest that adaptation of blood group-degrading enzymes to mucin structures in human colon ecosystems is chiefly by mutation-selection of comparatively small populations of constitutive enzyme-producing strains rather than by substrate induced enzyme synthesis in many strains.

ABO Blood-Group System↗
PubMed1976

[Electron microscopic detection of blood group antigen A on human erythrocytes by means of ferritin- and gold-labelled protectin of helix pomatia].

By means of ferritin- and gold-labelled protectin from the albumen gland of the edible snail Helix pomatia the blood group antigen A was located on human erythrocytes of groups A1, A2 and A1B. With erythrocytes of groups O and B the reaction is negative. The antigen is focally distributed on the outer surface of the cell membrane. Cells from groups A1 and A1B have an antigen A concentration about 4 times greater than A2 cells. The numbers of particles after tagging with ferritin or gold are comparable. The gold particles show an extremely high contrast and are therefore very suitable for the immunoelectron microscopic localization of antigens.

ABO Blood-Group System↗