Download e-book for kindle: Human Blood Groups: Chemical and Biochemical Basis of by Helmut Schenkel-Brunner

By Helmut Schenkel-Brunner

This monograph covers the total box of blood team serology, with its major emphasis at the chemical and biochemical foundation of blood staff specificity. complete attention is given to molecular biology investigations, particularly to experiences at the constitution of blood staff genes and the molecular organic foundation of alleles and infrequent blood workforce variations, wherein suitable literature as much as and together with 1994 is roofed. The textual content is supplemented by way of a number of illustrations and tables, and particular reference lists. This publication bargains a concise survey to be used through blood bankers and researchers in biochemistry, blood staff serology, immunohematology, forensic drugs, inhabitants genetics, and anthropology.

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2~3/6 N-acetylneuraminyltransferases which attach the chain-terminating sialic acid residues are localised in the trans-Golgi reticulum [21,22). The factors which control the synthesis of a distinct chain type have not yet been investigated. It must be assumed, however, that the pathway according to which a high-mannose type chain or a complex-type chain is formed is primarily determined by the accessibility of the carbohydrate chain to the action of the mannosidases (comp. [6,10]). -N-acetylgalactosamine to the hydroxyl groups of serine and threonine residues of the carrier protein (see Chapter 2).

Pure anti-B specific lectins have thus far been found only in fungi, such as Polyporus [= Fomes] fomentarius [264] or Marasmius oreades [96]. Some plant lectins agglutinate both A and B erythrocytes. Among those 'bifunctional' lectins the 'lectin I' of Bandeiraea (= GriHonia) simplicifolia [262] is best characterised [132,291,454]. It is a tetrameric molecule built out of two different subunits - one of them reacting primarily with blood group A structures (subunit A) and the other binding to blood group B determinants (subunit 8).

Gascard, P. (1992): Regulation and post-translational modification of erythrocyte membrane and membrane-skeletal proteins. Sem. Hematol 29, 244-292. 11. , Mikkelsen, A. & Branton, D. (1986): The molecular basis of erythrocyte shape. Science 234, 1217-1223. 12. , Steck. T. H. (1971): Electrophoretic analysis of the major polypeptides on the human erythrocyte membrane. Biochemistry 10, 2606-2617. 13. M. (1982): Interactions between membrane skeleton proteins and the intrinsic domain of the erythrocyte membrane.

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