Human Blood Groups: Chemical and Biochemical Basis of by Helmut Schenkel-Brunner

By Helmut Schenkel-Brunner

This monograph covers the full box of blood staff serology, with its major emphasis at the chemical and biochemical foundation of blood workforce specificity. complete attention is given to molecular biology investigations, specifically to reports at the constitution of blood staff genes and the molecular organic foundation of alleles and infrequent blood workforce editions, wherein correct literature as much as the 12 months 2000 is roofed. The textual content is supplemented by means of quite a few illustrations and tables, and specified reference lists.

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3: Dolichol and the precursor oligosaccharide as bound to dolichol pyrophosphate. Dol - PP - (GlcNAc) 2 - Man. :~ 1,/ H--N #O----------H B/" H V Glc y ) "'C~ 1 . . 4: Transfer of the lipid-bound precursor oligosaccharide to protein. Proposed catalytic mechanisms involving a hydrogen bond between the side chains of asparagine and the hydroxy amino acid in the 'acceptor sequence' Asn-Xaa-Thr(Ser). Reproduced from Bause and Legler (2) by permission of the Biochemical Society and Portland Press. London.

PAULSON, J. C. (1989): Conversion of Golgi apparatus sialyltransferase to a secretory protein by replacement of the NH 2 -terminal Signal anchor with a signal peptide. J. Bioi. 264, 17619-17622. 8. , VITALE, A. & CHRISPEELS, M. J. (1986): The position of the oligosaccharide side-chains of phytohemagglutinin and their accessibility to glycosidases determines their subsequent processing in the Goigi. Eur. J. Biochem. 158, 655-661. 9. HAKOMORI, S. I. (1989): Aberrant glycosylation in tumors and tumor-associated carbohydrate antigens.

LIu, S. C. (1991): Deletion in erythrocyte band 3 gene in malaria-resistant Southeast Asian ovalocytosis. Proc. Nat!. Acad. Sci. USA 88, 11022-11026. 25. , RUBIN, H. , PRCHAL, J. , KORSGREN, C. & COHEN, C. M. 2. Blood 80, 523-529. 26. , RUBIN, H. , ZOLOTAREV, A. , ALPER, S. , 51 4 ERYTHROCYTE MEMBRANE WICHTERLE, H. & PALEK, J. (1995): Mutations of conserved arginines in the membrane domain of erythroid band 3 lead to a decrease in membrane-associated band 3 and to the phenotype of hereditary spherocytosis.

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