By Gary Walsh

Pharmaceutical Biotechnology deals scholars taking Pharmacy and similar scientific and Pharmaceutical classes a complete creation to the fast-moving zone of biopharmaceuticals. With a selected concentrate on the topic taken from a pharmaceutical point of view, preliminary chapters supply a large creation to protein technology and recombinant DNA know-how- key components that underpin the full topic. next chapters concentration upon the advance, creation and research of those elements. ultimately the publication strikes directly to discover the technological know-how, biotechnology and scientific purposes of particular biotech items different types. those contain not just protein-based components but additionally nucleic acid and cell-based items.

  • introduces crucial rules underlining sleek biotechnology- recombinant DNA know-how and protein science
  • an precious advent to this fast-moving topic aimed in particular at pharmacy and clinical students
  • includes particular ‘product type chapters’ concentrating on the pharmaceutical, clinical and healing houses of diverse biopharmaceutical products.
  • entire bankruptcy dedicated to the rules of genetic engineering and the way those medications are developed.
  • includes various correct case reviews to reinforce scholar understanding
  • no past wisdom of protein constitution is assumed 

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Extra resources for Pharmaceutical Biotechnology. Concepts and Applications

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Nature Biotechnology 24, 1241–1252 Role/effect Comment Protein folding Glycosylation can effect local protein secondary structure and help direct folding of the polypeptide chain The glycocomponent can participate in the sorting/ directing of a protein to its final destination The carbohydrate content of antibodies, for example, plays a role in antibody binding to monocyte Fc receptors and interaction with complement component C1q The carbohydrate side chain of gonadotrophins is essential to the activation of gonadotrophin signal transduction Sugar side chains can potentially stabilize a glycoprotein in a number of ways, including enhancing its solubility, shielding hydrophobic patches on its surface, protection from proteolysis and by direct participation in intrachain stabilizing interactions High levels of sialic acid (a family of acidic sugars that often caps sugar side chains) can increase a glycoprotein’s plasma half-life.

Man: manose; Gal: galactose; SA: sailic acid; GlcNAc: N-acetyl glucosamine; GalNAc: N-acetyl galactosamine that a proportion of the glycosylated proteins may be exported from the cell before they are fully processed by glycosyltransferases. Virtually all therapeutic glycoproteins, even when produced naturally in the body, exhibit such heterogeneity; for example, two species of human interferon-γ (IFN-γ), one of molecular mass 20 kDa and the other of 25 kDa, differ from each other only in the degree and sites of (N-linked) glycosylation.

Imperiali, B. and O’Connor, S. 1999. Effect of N-linked glycosylation on glycopeptide and glycoprotein structure. Current Opinion in Chemical Biology 3(6), 643–649. Lee, B. and Vasmatis, G. 1997. Stabilization of protein structures. Current Opinion in Biotechnology 8, 423–428. McLihnney, R. 1990. The fats of life; the importance and function of protein acylation. Trends in Biochemical Sciences 15, 387–391. Merry, T. 1999. Current techniques in protein glycosylation analysis – a guide to their application.

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