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Pharmacology of Hydroxyethyl Starch. John M. Mishler

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We selected an 8-azaguanine-resistant variant of a human myeloma cell line (RPMI 8226) by cloning the parental cells on a feeder layer of mouse spleen cells in the presence of increasing concentrations of 8-azaguanine. Culture media and cellfree extracts of both the parental and variant (8226 AR/NIP4-1) cell lines were assayed for production of immunoglobulin heavy and light chains by double immunodiffusion and for lambda-chain by radioimmunoassay. Secretion of free lambda-chain by the parental cell line was confirmed. In contrast, no immunoglobulin heavy or light chains were detected in culture medium of the variant cell line by either immunodiffusion or radioimmunoassay. No intracellular lambda-chain could be detected in the variant cells by radioimmunoassay of cellfree extracts or by immunofluorescence of fixed cells. Hybridomas were produced by fusion of 8226AR/NIP4-1 cells with lymphocytes from a mesenteric lymph node recovered at surgery from a hypertransfused renal transplant recipient. Twenty hybrid culture supernatants were assayed for immunoglobulin by double immunodiffusion, and 15 contained either IgG (lambda) or IgG (kappa). None produced IgM or IgA. An IgG (kappa)-producing hybridoma was shown by immunofluorescence not to express lambda-chain. A second fusion between the variant cell line and spleen cells from a renal transplant patient produced a stable hybridoma secreting IgM (lambda) antibody specific for the I antigen.
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Four monoclonal antibodies produced by hybridomas obtained from a mouse immunized with a human adenocarcinoma cell line SW1116 (Koprowski, H., Steplewski, Z., Mitchell, K., Herlyn, M., Herlyn, D., and Fuhrer, P. (1979) Somatic Cell Genet. 5, 957-972) are directed against the Leb antigen of the human Lewis blood group system. Their specificities were established by binding studies using purified Leb-active ceramide hexasaccharide and by hapten inhibition studies involving oligosaccharides obtained from human milk.
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It is shown that S-s-U-erythrocytes have no detectable PAS-3, B- and C-glyco-protein bands which are demonstrable by SDS-polyacrylamide gel electrophoresis of red cell membranes and subsequent PAS-staining. PAS-1 and -2 are normal with respect to electrophoretic mobility and staining intensity. The staining intensity of PAS-3, B and C from heterozygous defective erythrocytes is about half of normal. One S-s-U+ blood sample did not differ from the S-s-U-bloods.
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Sodium dodecylsulphate polyacrylamide gel electrophoretic methods and quantitative analyses of the N-terminal amino acids were applied to the sialoglycoprotein mixture and glycoprotein fractions from normal erythrocyte membranes, as well as preparations from red cells of individuals belonging to the English and Finnish En(a-) families. The data confirm the observation by alternative methods that SS cells exhibit a higher Ss glycoprotein content than ss erythrocytes. The results of end-group analyses suggest that the N-terminal amino acids serine and leucine represent the structures differentiating the MN and the 'M' and 'N' antigens on the MN and Ss glycoproteins respectively. Data from peptide sequence analyses confirm that the glycine/glutamic acid polymorphism at the fifth position of the MN glycoprotein's peptide chain is closely or absolutely linked with the serine/leucine polymorphism at its N-terminal position. As normal (EnaEna) red cells exhibiting 'M' antigenic properties have not been detected, the hypothesis is proposed that the Ss glycoprotein of English En(a-) erythrocytes possesses an MN-Ss hybrid polypeptide chain analogous to those of the delta-beta Lepore haemoglobins.
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En(a-) and EnaEn red cells from different sources were studied using biochemical and serological methods. The results suggest that Finnish En(a-) erythrocytes contain only "N" but no M antigenic properties. Data on the members of the English En(a-) family suggest that English En(a-) red cells exhibit a combination of three rare alterations. The English En(a-) individuals are apparently heterozygous for the defects En and Ms, to all appearances, converted to a M ("M") antigen. These extraordinary data are brought to light by investigations on the children of the propositus (G.P. and J.P.), whose red cells are M-N+S-s+"N"+"M"- and M-N+S+s+"N"+"M"+ respectively. Sodium dodecylsulphate polyacrylamide gel electrophoretic results indicate that the MN glycoprotein content is decreased by about 50% in all English S+s+EnaEn red cells, the Ss glycoprotein being normal. G.P. erythrocytes, however, have only about half of the normal MN and Ss glycoprotein content.
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THE manufacture of predefined specific antibodies by means of permanent tissue culture cell lines is of general interest. There are at present a considerable number of permanent cultures of myeloma cells1,2 and screening procedures have been used to reveal antibody activity in some of them. This, however, is not a satisfactory source of monoclonal antibodies of predefined specificity. We describe here the derivation of a number of tissue culture cell lines which secrete anti-sheep red blood cell (SRBC) antibodies. The cell lines are made by fusion of a mouse myeloma and mouse spleen cells from an immunised donor. To understand the expression and interactions of the Ig chains from the parental lines, fusion experiments between two known mouse myeloma lines were carried out.
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Peripheral-blood mononuclear cells from an individual known to produce antibody to the rhesus D blood group were enriched for specific antibody-producing cells before transformation with Epstein-Barr virus. An anti-rhesus-D antibody-producing cell line (UCH D4) was obtained and cloned. Culture supernatants contained about 20 micrograms/ml of rhesus-D-specific IgG-class antibody. The antibody reactivity compared well with that of reagents used routinely for rhesus blood-grouping.
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Two examples of mouse monoclonal anti-N are described. The antibodies were derived from mice immunized with sialoglycoprotein extracts of group O MM ss erythrocyte membranes and the probable stimulus for immunization was glycophorin B associated N-antigen. Both antibodies reacted as direct agglutinins but appeared to recognize different epitopes with one having a greater dependence on sialic acid. The antibodies could prove to be valuable alternatives to those reagents used currently for N-blood grouping.
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The precise physicochemical conditions under which two examples of mouse monoclonal anti-N can be used as blood grouping reagents have been defined. The antibodies were shown to belong to the IgG1 and IgG2b subclasses respectively and both reacted within discrete ranges of temperature and pH with optimal reactions occurring at 20 degrees C or less and pH 8.5. Under these conditions and at concentrations of 2-3 micrograms/ml, the antibodies were used, in parallel with conventional polyclonal antisera, to type a series of random blood donors. The results obtained with one of the monoclonal antibodies and the polyclonal reagents were in perfect agreement and the monoclonal antibody was judged to have considerable potential as an N-grouping reagent.
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The serum of J.R. contains anti-Wrb and her red blood cells are of the phenotype Wr(a-b-). Evidence was obtained that suggested that her cells totally lack normal MN and Ss sialoglycoproteins (SGPs), and carry instead an abnormal SGP, which is likely to be a hybrid SGP resembling the MN SGP in its outer portion and the Ss SGP in its inner portion. Although the apparent hybrid SGPs of J.R. and the MiV homozygote are virtually indistinguishable in terms of their electrophoretic mobility (apparent molecular weight 40,000) and staining characteristics, they are not identical. That of J.R. is associated with a weak M and increased S antigen, while that of the MiV homozygote is associated with a very weak N, a greatly exalted s, and the rare antigen, Hil. Like the study on the blood of the MiV homozygote, serologic studies on the red blood cells of J.R. have revealed considerable heterogeneity of what have previously been called the Ena antigen and anti-Ena antibodies.
Blood bank quality assurance Blood group immunology: theoretical and practical concepts. Miami, F L Dade Division, American Hospital Supply Corporation, 1976: 148. 27. lssitt PD. lssitt CH. Applied blood group serology
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Langley JW, lssitt PD, Anstee DJ, et al. Another individual (J.R.) whose red blood cells appear to carry a hybrid MNSs sialoglycoprotein. Transfusion 1981;21: 15-24. 678-82. Book Review 29. Steck TL. The organization of proteins in the human red blood cell membrane. J Cell Biol 1974;62:1-19.
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Dahr W, lssitt PD, Uhlenbruck G. New concepts of the MNS blood group system. In: Mohn JF, ed. Human blood groups. Basel: Karger, 1977:197-205.
American Red Cross Blood Services, Missouri/ Illinois Region American Red Cross Blood Services, Missouri/IIlinois Region
  • Robert W Allen
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-Robert W. Allen, PhD, American Red Cross Blood Services, Missouri/ Illinois Region, 4050 Lindell Blvd., St. Louis, MO 63 108. [Reprint requests] Nancy Nunley, BS, American Red Cross Blood Services, Missouri/ Illinois Region. Mary Ellen Kimmeth, MT(ASCP), American Red Cross Blood Services, Missouri/IIlinois Region. Mary Wallhermfechtel, SBB(ASCP), American RedCross Blood Services, Missouri/lllinois Region. Virginia Vengelen-Tyler, MT(ASCP)SBB, American Red Cross Blood Services, Los Angeles-Orange County Region, I130 So. Vermont Ave., Los Angeles, CA 90006.
Applied blood group serology
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lssitt PD. lssitt CH. Applied blood group serology. 2nd ed. Oxnard, CA: Spectra Biologicals, 1975:25.
American Red Cross Blood Services, Missouri/IIlinois Region
  • Mary Ellen Kimmeth
Mary Ellen Kimmeth, MT(ASCP), American Red Cross Blood Services, Missouri/IIlinois Region.
American Red Cross Blood Services, Missouri/ Illinois Region, 4050 Lindell Blvd
  • Robert W Allen
Robert W. Allen, PhD, American Red Cross Blood Services, Missouri/ Illinois Region, 4050 Lindell Blvd., St. Louis, MO 63 108.
Applied blood group serology
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lssitt PD. lssitt CH. Applied blood group serology. 2nd ed. Oxnard, CA: Spectra Biologicals, 1975:25.
Book Review 29. Steck TL. The organization of proteins in the human red blood cell membrane
Book Review 29. Steck TL. The organization of proteins in the human red blood cell membrane. J Cell Biol 1974;62:1-19.
SDS-polyacrylamide gel electrophoretic analysis of the membrane glycoproteins from S-S-U-erythrocytes
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Dahr W, Uhlenbruck G, lssitt PD, Allen FH. SDS-polyacrylamide gel electrophoretic analysis of the membrane glycoproteins from S-S-U-erythrocytes. J lmmunogenet 1975;2:249-51.
American RedCross Blood Services, Missouri/lllinois Region
  • Mary Wallhermfechtel
Mary Wallhermfechtel, SBB(ASCP), American RedCross Blood Services, Missouri/lllinois Region.