Glycotechnology
Editat de E. G. Berger, H. Clausen, Richard D. Cummingsen Limba Engleză Paperback – 13 oct 2012
Glycotechnology serves as an excellent reference, providing insight into some of the most challenging research issues in the field.
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| Paperback (1) | 902.70 lei 43-57 zile | |
| Springer Us – 13 oct 2012 | 902.70 lei 43-57 zile | |
| Hardback (1) | 848.05 lei 38-44 zile | |
| Springer Us – 30 oct 1999 | 848.05 lei 38-44 zile |
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Specificații
ISBN-13: 9781461373971
ISBN-10: 1461373972
Pagini: 108
Ilustrații: VI, 100 p.
Dimensiuni: 210 x 280 x 6 mm
Greutate: 0.26 kg
Ediția:Softcover reprint of the original 1st ed. 1999
Editura: Springer Us
Colecția Springer
Locul publicării:New York, NY, United States
ISBN-10: 1461373972
Pagini: 108
Ilustrații: VI, 100 p.
Dimensiuni: 210 x 280 x 6 mm
Greutate: 0.26 kg
Ediția:Softcover reprint of the original 1st ed. 1999
Editura: Springer Us
Colecția Springer
Locul publicării:New York, NY, United States
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Public țintă
ResearchDescriere
Glycotechnology brings together in one place important contributions and up-to-date research results in this fast moving area.
Glycotechnology serves as an excellent reference, providing insight into some of the most challenging research issues in the field.
Glycotechnology serves as an excellent reference, providing insight into some of the most challenging research issues in the field.
Cuprins
Genetic engineering of recombinant glycoproteins and the glycosylation pathway in mammalian host cells; E. Grabenhorst, P. Schlenke, S. Pohl, M. Nimtz, H.S. Conradt. Filamentous fungi as production organisms for glycoproteins of biomedical interest; M. Maras, I. van Die, R. Contreras, C.A.M.J.J. van den Hondel. Insect cells as hosts for the expression of recombinant glycoproteins; F. Altmann, E. Staudacher, I.B.H. Wilson, L. März. The yeast expression system for recombinant glycosyltransferases; M. Malissard, S. Zeng, E.G. Berger. Synthesis of oligosaccharides by bacterial enzymes; K.F. Johnson. Enzymatic synthesis of nucleotide sugars; T. Bülter, L. Elling. Substrate and donor specificity of glycosyl transferases; B. Ernst, R. Oehrlein. The Acceptor specificity of UDP-GalNAc: Polypeptide N-Acetylgalactosaminyltransferases; Å.P. Elhammer, F.J. Kézdy, A. Kurosaka.