In order to find out whether or not the incidence rate of RhD-immunization has increased in pregnant women who were not given antenatal prophylaxis a survey was carried out comprising 620 women. It was evident that the number of new immunizations had decreased, both in absolute numbers and in relation to the number of births during the years 1991-1998. Hence prophylactic anti-D seems not to be indicated, neither for this group of women nor for women who have had a spontaneous abortion.

International Journal of ImmunogeneticsVolume 17, Issue 4-5 p. 279-299 ABO ANTIBODIES—SEROLOGICAL BEHAVIOUR AND IMMUNO-CHEMICAL CHARACTERIZATION R. Oriol, Corresponding Author R. Oriol Biochimie. Faculté de Pharmacie, Châtenay-Malabry, FranceR. Oriol, Biochimie, Faculté de Pharmacie, Wniversité de Paris Sud, F-92296 Châtenay-Malabry, France.Search for more papers by this authorB. E. Samuelsson, B. E. Samuelsson Department of Medical Biochemistry and Regional Blood Centre, Sahlgrenska Hospital, University of Göteborg, SwedenSearch for more papers by this authorL. Messeter, L. Messeter University Hospital Blood Centre, Lund, SwedenSearch for more papers by this author R. Oriol, Corresponding Author R. Oriol Biochimie. Faculté de Pharmacie, Châtenay-Malabry, FranceR. Oriol, Biochimie, Faculté de Pharmacie, Wniversité de Paris Sud, F-92296 Châtenay-Malabry, France.Search for more papers by this authorB. E. Samuelsson, B. E. Samuelsson Department of Medical Biochemistry and Regional Blood Centre, Sahlgrenska Hospital, University of Göteborg, SwedenSearch for more papers by this authorL. Messeter, L. Messeter University Hospital Blood Centre, Lund, SwedenSearch for more papers by this author First published: August 1990 https://doi.org/10.1111/j.1744-313X.1990.tb00880.xCitations: 47AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onFacebookTwitterLinked InRedditWechat Citing Literature Volume17, Issue4-5August 1990Pages 279-299 RelatedInformation

International Journal of ImmunogeneticsVolume 17, Issue 4-5 p. 343-345 THE FUTURE OF MABS WORKSHOPS AND THE FUTURE OF BLOOD BANKS B. E. Samuelsson, Corresponding Author B. E. Samuelsson Department of Medical Biochemistry and Regional Blood Center, Sahlgren's Hospital, University of Göteborg, SwedenB.E. Samuelsson, Department of Medical Biochemistry, and Regional Blood Center, University of Goteborg, Sweden.Search for more papers by this authorL. Messeter, L. Messeter University Hospital Blood Center, Lund, SwedenSearch for more papers by this author B. E. Samuelsson, Corresponding Author B. E. Samuelsson Department of Medical Biochemistry and Regional Blood Center, Sahlgren's Hospital, University of Göteborg, SwedenB.E. Samuelsson, Department of Medical Biochemistry, and Regional Blood Center, University of Goteborg, Sweden.Search for more papers by this authorL. Messeter, L. Messeter University Hospital Blood Center, Lund, SwedenSearch for more papers by this author First published: August 1990 https://doi.org/10.1111/j.1744-313X.1990.tb00886.xAboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onFacebookTwitterLinked InRedditWechat Volume17, Issue4-5August 1990Pages 343-345 RelatedInformation

Several monoclonal antibodies (MAbs) directed to blood group P1 (Gal alpha 1-4Gal beta 1-4GlcNAc beta-O) and Pk (Gal alpha 1-4Gal beta 1-4Glc beta-O) determinants were produced with high efficiency by using synthetic neoglycoproteins as immunogens. The specificity of IgM and IgG1 MAbs was characterized by binding to defined oligosaccharides and glycoconjugates. Antibodies that bound equally well to P1 and Pk determinants and to Gal alpha 1-4Gal beta 1-O-derivatives were obtained, together with others that showed selective recognition of the entire trisaccharide chain. Selected antibodies were shown to be useful as reagents for detection of the blood group P antigens in glycolipid extracts of erythrocytes and on the surface of erythrocytes of different P phenotypes, demonstrated both by radioimmune assays and hemagglutination. Six IgM MAbs directed to the Pk determinant bound selectively to Burkitt lymphoma cells and 2 of these antibodies (424/3D9 and 424/6A2) could be used as auxiliary reagents in immunofluorescence for diagnosis and classification of B-cell lymphomas and leukemias using flow cytometric analysis. Eight normal individuals and 37 patients with lymphoma or leukemia were studied. Tumor cells of 2/2 patients with "Burkitt-like" lymphoma, 1 patient with centroblastic lymphoma and 2 patients with acute leukemia were strongly stained for the Pk antigen. The staining patterns for differentiation markers classified the tumor cells to a developmental stage closely related to the Burkitt cell type.

Seven antibodies gave agglutination patterns expected of anti-H antibodies. Two of these (3 W 1, 11 W 5) were anti-H type 2 in ELISA, whereas others (5 W 9, 9 W 6, 11 W 4, 34 W 4) showed more or less pronounced cross reactivity, mainly with the Y antigen. Two antibodies (5 W 9, 11 W 4) actually were seemingly pure anti-Y's. One antibody (9 W 7) was very weak and did not bind to any antigen in the ELISA test. On the other hand, one antibody (34 W 3) was in the ELISA mainly an anti-Y but a non specific panagglutinin in hemagglutination tests. Two antibodies (9 W 8, 34 W 6) recognized the Lea and another two (5 W 6, 34 W 2) the Leb antigen. None of the antibodies was strong, and all but one (34 W 2) were specific in hemagglutination tests. The anti-Lea antibodies gave weak cross reactions in the ELISA, whereas the anti-Leb's gave rather broad cross reactions. Two antibodies (9 W 8, 27 W 6) behaved as anti-I in hemagglutination but did not bind to any of the structures in the ELISA. Four antibodies behaved in hemagglutination as anti-P 1 (16 W 4), anti-P ? (5 W 7) and anti-Pk ? (27 W 2, 34 W 5), respectively. Only the anti-P 1, which was weak, could be confirmed in the ELISA, whereas the other three antibodies did not bind to any of the relevant structures. One antibody (27 W 3) was a strong panagglutinin but bound to none of the glycoconjugates in the ELISA. Another antibody (32 W 5) gave reactions as a weak anti-A and a third (38 W 2) as an anti-Pr. The latter did not bind to the sialylated structure in the ELISA. The last antibody (38 W 1) bound very weakly to most of the glycoconjugates but had no demonstrable activity in hemagglutination tests. Thus, few of these antibodies were completely specific both in hemagglutination and in the ELISA test, and those that were specific were often rather weak. Therefore, only a few of these antibodies would be suitable for routine phenotyping of red cells. For other purposes, such as immuno-histology, some antibodies could probably be very useful. However, their reaction patterns and binding to different glycoconjugates would to be studied very carefully before use in order to avoid misleading or incorrect results.

A mouse monoclonal antibody (425/2B, IgM) was obtained which shows specificity for blood group M determinant of glycophorin A. The antibody is pH-dependent. At pH 6–7 it reacted strongly with blood group M antigen, but also cross-reacted distinctly with N antigen. At pH 8.3 the antibody showed moderately decreased reactivity with M antigen, but no interaction with N antigen was detectable by hemagglutination, immunoblotting, or microplate ELISA. The direct binding studies and inhibition of 425/B antibody by untreated or modified blood group M and N glycoproteins or tryptic glycopeptides showed that the binding to the antigens was not affected by acetylation of their amino groups, or removal of amino-terminal amino acid residue. Desialylation of the antigens decreased their reactivity with the antibody and this effect was distinctly stronger at pH 7 than 8.3. The antibody reacted strongly at pH 7 and 8.3 with glycophorin B of Henshaw phenotype, whereas its reactivity with normal glycophorin B was weak or undetectable at these pH values, respectively. The results obtained indicated that anti-M specificity of 425/2B antibody is related to the 5th amino acid residue of glycophorin A (anti-Mgly specificity) and that pH shift from 7 to 8.3 changes the fine specificity of the antibody. At pH 8.3 the reactivity of the antibody is more dependent on glycine residue (higher anti-M specificity) and less dependent on sialic acid residues in the antigen.

The antibody must be completely specific. Non specific hemagglutination reactions must not occur at any temperature or after enzyme treatment of A or O red cells. Titer must be satisfactory, i.e. 128 or more with B, A1B and A2B red cells. Avidity must be high and comparable to the best polyclonal reagent, i.e. agglutination must start within a few seconds and be complete in about 30 seconds, also B and A1B cells. The antibody must give good agglutination reactions with cord cells and preferably also with weak variants.

A haemagglutinating monoclonal anti-LebL antibody has been obtained from a mouse-mouse hybridoma after immunization with the Leb-active oligosaccharide lacto-N-difucohexaose I, coupled to edestin. Of 13 other antibodies obtained, one was able to agglutinate enzyme-treated erythrocytes of all ABO groups and three more were considered to be anti-LebH haemagglutinins. The remaining nine antibodies did not agglutinate red cells. The specificity of the stronger of the anti-LebL haemagglutinins was examined by studying its binding to a number of glycoconjugates and oligosaccharides.

A series of fusions using mouse myeloma cells and spleen cells from mice immunized with blood group substances or human red cells was performed with the aim of obtaining ABO antibodies suitable for routine blood grouping. Seven strongly agglutinating antibodies against antigens in the ABO system were obtained from 18 fusions. These antibodies were tested extensively in manual and automated routines, and six of them were found to be as good as or better than commercial polyclonal test sera of human origin.

Vox SanguinisVolume 46, Issue s1 p. 98-100 Delayed Haemolytic Transfusion Reactions: An Indication for Improvement in Technique? Dr. Lisbeth Messeter, Corresponding Author Dr. Lisbeth Messeter University Hospital, Blood Bank, Lund, Sweden*Blood Bank, University Hospital, S-221 85 Lund (Sweden)Search for more papers by this author Dr. Lisbeth Messeter, Corresponding Author Dr. Lisbeth Messeter University Hospital, Blood Bank, Lund, Sweden*Blood Bank, University Hospital, S-221 85 Lund (Sweden)Search for more papers by this author First published: April 1984 https://doi.org/10.1111/j.1423-0410.1984.tb00135.xAboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL No abstract is available for this article. Volume46, Issues1April 1984Pages 98-100 RelatedInformation

Vox SanguinisVolume 46, Issue s1 p. 101-103 Recommendations from Session 6 Dr. Lisbeth Messeter, Corresponding Author Dr. Lisbeth Messeter University Hospital Blood Bank, Lund, Sweden*Blood Bank, University Hospital, S-221 85 Lund (Sweden)Search for more papers by this authorG.W.G. Bird, G.W.G. Bird University of Birmingham, Birmingham, UKSearch for more papers by this author Dr. Lisbeth Messeter, Corresponding Author Dr. Lisbeth Messeter University Hospital Blood Bank, Lund, Sweden*Blood Bank, University Hospital, S-221 85 Lund (Sweden)Search for more papers by this authorG.W.G. Bird, G.W.G. Bird University of Birmingham, Birmingham, UKSearch for more papers by this author First published: April 1984 https://doi.org/10.1111/j.1423-0410.1984.tb00136.xCitations: 2AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onEmailFacebookTwitterLinkedInRedditWechat No abstract is available for this article.Citing Literature Volume46, Issues1April 1984Pages 101-103 RelatedInformation

The sera of 96 consecutive Rh-negative female infants born to Rh-positive mothers were examined at birth, and sera from 88 of these infants were examined for the presence of Rh-antibodies at the ages of about three and eight months. A two-stage papain test and an AutoAnalyzer method were used for antibody screening and identification. Weak anti-D antibodies were found by the papain and AutoAnalyzer techniques in two cord sera, In neither case could the antibodies be demonstrated in samples taken on later occasions. Weak anti-D antibodies were found by the AutoAnalyzer technique but not by the manual methods in the sera of two other infants at the age of eight months. These antibodies could still be demonstrated by the same technique in samples taken about one month later. Though far from conclusively, the results support the "grandmother theory", but because of the low incidence of sensitization and uncertain nature of the anti-D antibodies demonstrable only by the AutoAnalyzer technique, anti-D prophylaxis is not recommended for newborn Rh-negative female infants with Rh-positive mothers.

Human erythrocyte membranes of different blood-group-P phenotypes have been degraded by trifluoroacct olysis at conditions that will effect transamidation. This degradation resulted in dissolution of the membranes with concomitant degradation of proteins. Oligosaccharide chains linked to proteins and ceramides were released as their pertrifluoroacetylated derivatives, which generally are stable towards further action of the reagent. 2-Acetamido-2-deoxy-sugar residues were converted into their corresponding 2-deoxy-2-trifluoroacetamido derivatives. The mixture of pertrifluoroacetylated oligosaccharides obtained was de-O-trifluoroacetylated and de-N-trifluoroacetylated, reduced, acetylated, permethylated and analyzed by gas-liquid chromatography/mass spectrometry. Membranes obtained from two individuals with phenotype B, p̄ (known to contain an excess of lactosyl ceramide) gave almost identical results with lactose released as the main component. From AZB, Pk1 cell membranes small amounts of lactose were obtained but the trisaccharide Gal(α1-4)Gal(β1-4)Glc was the major component found. This trisaccharide is most likely derived from the Pk antigen (trihexosyl ceramide). Membranes from a donor with the phenotype B.P1 yielded small amounts of both lactose and the Pk trisaccharide together with a larger quantity of the tetrasaccharide GalNAc(β1-3)Gal(α1-4)Gal(β1-4)Glc. The tetrasaccharide represents the carbohydrate portion of the P antigen (globoside). From all three types of membranes the B-specific trisaccharide Gal(α1-3)Gal was obtained. This compound is probably derived from specific degradation of blood-group-B-active glycoproteins and/or glycolipids. In addition to the oligo-saccharides mentioned above a large number of others were observed but in lower amounts.

The effect of oral administration of galactose, lactose, and sucrose and intravenous injection of galactose on the urinary excretion of blood-group-active oligosaccharides has been studied. Galactose given either as the free sugar, a glycoside (lactose) or a constituent of normal diet was an absolute requirement for the formation and excretion of A-trisaccharide, B-trisaccharide and 2'-fucosylgalactose in blood group A, B and O(H) secretors, respectively. Great individual variation was seen in the amounts of galactose-dependent oligosaccharides excreted. Injection of galactose resulted in excretion of 3-59% of the amount of oligosaccharide formed after oral administration to the same individual. The mean ratio A-trisaccharide/B-trisaccharide was 2.7 in four blood-group-A1B secretors and 0.22 in three A2B secretors and can thus serve as a parameter for chemical differentiation between the two blood groups. The excretion of larger blood-group-active oligosaccharides, including the A-pentasaccharide, the B-pentasaccharide and lactodifucotetraose, that are normal components in urine from, respectively, starved A, B, and H secretors, was about the same after oral administration of galactose or lactose. The B-trisaccharide was the only oligosaccharide detected in plasma after oral galactose administration to a blood-group-B secretor individual. The concentration was 0.38 mg/l of plasma.

La sensibilité du dépistage des anticorps ne se révèle pas tout à fait satisfaisante sur les équipements Groupamatic 360. Une des explications possibles serait que la machine apporte une certaine dilution et une distribution inégale des échantillons. De plus, le traitement en un temps par la broméline des globules-tests n'est pas optimal.