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At least 19 recordsLinked to original sources
PubMed1975

[Blood group specific properties of leucocyte nuclei (author's transl)].

The absorbing and precipitating capacity of leucocyte nuclear suspensions derived from conserved blood of various blood groups was examined with anti-A-, anti-B-, anti-H, anti-M-, anti-N-, and anti-CDE-, and anti-D-sera as well as with anti-AHP- and Evonymus-extracts. Nuclei of blood group A absorbed anti-A, but not anti-B; nuclei of blood group B absorbed anti-B, but not anti-A. Nuclei of blood group 0 absorbed anti-H, but neither anti-A nor anti-B. Anti-M-, anti-N-, anti-CDE-, and anti-D-sera showed no absorption effect after incubation with leucocyte nuclei of corresponding blood groups. A nuclei were strongly precipitated by anti-AHP; B- and 0-nuclei were markedly precipitated by Evonymus-extract. B- and 0-nuclei showed only a weak precipitation with anti-AHP-extract; A-nuclei were only slightly precipitated by Evonymus-extract. Hence, leucocyte nuclei possess blood group specific properties, which, according to the present studies, are limited to certain blood group systems.

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↗
PubMed1975

Effect of carbamylation of lysine epsilon-amino groups on the activity of blood group specific glycoproteins.

Carbamylation of epsilon-amino groups of lysine of human blood group MM glycoprotein, some of its precursors and the blood group A B antigens gave products with 41% - 91% epsilon-amino group substitution. Even the most extensive carbamylation led to only marginal changes in the circular dichroic (CD) spectra of these substances and none in sedimentation coefficients studied. Nevertheless, carbamylation resulted in either increased or unchanged or decreased inhibitory activity of all blood group antigens tested depending solely on the source of the hemagglutinin used. Carbamylation of epsilon-amino groups of these blood group glycoproteins therefore leads to minor conformational changes, not involved with the primary blood group specificity, which is recognized by a large proportion but not by all corresponding antibodies and lectins.

ABO Blood-Group System↗
PubMed1976

Blood group MN precursors as human breast carcinoma-associated antigens and "naturally" occurring human cytotoxins against them.

Blood groups MN active substances were found in benign and malignant human mammary glands. However, the precursor T (Thomsen-Friedenreich) antigen, as determined with human sera, occurred in all cancerous breast tissues tested but not in the benign mammary glands. Anti-T antibody, which is present in all human sera, was severely depressed in 21.16% of 189 breast carcinoma patients, compared with 3.62% of 470 persons of similar age without cancer. Of 720 persons tested approximately 85% of those with severely depressed anti-T had carcinoma; their IgG, IgM and IgA concentrations were of normal range. A greater than 25%-90% increase in anti-T titer score was found in 65.6% of 32 patients bled 1-14 months after mastectomy for carcinoma as compared with 3.1% of 32 patients with breast biopsy who had no carcinoma. All differences in anti-T titer score changes reported are statistically highly significant. Injection of T antigen from human erythrocytes increased anti-T titer scores.

Adolescent↗
PubMed1978

Concerning the linkage relationships of the Gc and MNSs loci.

Lod scores for the linkage relationships of the Gc and MNSs loci are presented for data from a number of published pedigrees and 103 new families. Linkage may be excluded at a recombination frequency of less than 25% in males and 30% in females.

Alpha-Globulins↗
PubMed1976

Studies on the receptors of the MNSs group system.

Results with modified human red cell membrane sialoglycoproteins indicate that alkali-labile sialic acid and amino groups are parts of the erythrocyte receptor sites recognized by common rabbit and human anti-M and -N sera. The "N" antigen, demonstrable in MM glycoprotein preparations by rabbit anti-N, has structural properties which are similar to those of the MN receptors. Sialic acid, amino groups and carbohydrate, susceptible to periodate oxidation, are not involved in the Ss antigen sites. The specificity of the Vicia graminea lectin is dependent on free amino and carboxyl groups. Its affinity for the substances is increased by blocking of amino groups.

Animals↗
PubMedDate not supplied

Formaldehyde in the pathogenesis of hemodialysis-related anti-N antibodies.

The role of formaldehyde (CH2O) in the pathogenesis of anti-N-like antibodies found in patients on chronic hemodialysis was investigated. In vitro studies were performed by incubating MM cells in varying concentrations of CH2O for variable time periods, corresponding to conditions that occur in dialysis. This MM cells acquired reactivity to anti-N antibody. The antigenic shift is felt to occur from the interaction of CH2O with the terminal N-acetylneuraminic acid (sialic acid) groups of M substance, resulting in the exposure to an altered-N antigen that is immunogenically active. Through a similar mechanism, CH2O may also directly modify N substance.

Antibodies↗
PubMed1978

Effect of periodate oxidation on specific activities and carbohydrate components of human blood group N- and M-specific glycoproteins and glycopeptides.

Mild as well as strong periodate oxidation of isolated erythrocyte N and M glycoproteins and glycopeptides gave extensive to complete destruction of N-specificities as measured with Vicia graminea extracts and of N- as well as M- activities determined with all but 1 of 8 animal anti-N and 13 anti-M sera. Results with human antisera differed somewhat, while the specificity of mildly oxidized N-glycoprotein was completely destroyed as determined with all 8 human anti-N sera used, that of strongly oxidized N-active substance was completely inactivated towards one of the human antisera; the remainder showed 63--94% destruction, and 2 sera indicated no effect of oxidation. Similarly, while 10 of 14 human anti-M indicated complete inactivation of M-specific glycoproteins and glycopeptides after mild or strong oxidation, 2 showed partial inactivation and 2 human anti-M sera showed no inactivating effect of oxidation. The most relevant findings of quantitative carbohydrate analysis of periodate oxidized N- and M-specific substance were extensive transformation of N-acetylneuraminic acid (NAN) to its C8 and C1 analogues on mild oxidation and pronounced destruction of NAN and its analogues on strong oxidation; however, some intact NAN always remained. In all instances galactose (Gal) was destroyed to a much larger extent in N-derived than in M-derived glycoproteins and glycopeptides.

Amino Acids↗