Stability of Protein Pharmaceuticals: Part B: In Vivo Pathways of Degradation and Strategies for Protein Stabilization / Edition 1

by Tim J. Ahern, Mark C. Manning

Overview

Part B explores protein degradation occuring in vivo during protein synthesis in cells, examines the isolation and purification of proteins, details protein use in organisms, and reviews techniques to enhance protein stability.

Product Details

ISBN-13:	9780306441530
Publisher:	Springer US
Publication date:	11/30/1992
Series:	Pharmaceutical Biotechnology , #3
Edition description:	1992
Pages:	328
Product dimensions:	6.14(w) x 9.21(h) x 0.36(d)

Table of Contents

Improper Glycosylation and the Cellular Editing of Nascent Proteins; D.A. Cumming. Protein Aggregation In Vivo; R. Wetzel. Pathways of Intracellular Protein Degradation in Eukaryotic Cells; T.S. Olson, et al. Effects of Aging on Proteins; R.W. Gracy. Engineering Dramatic Increases in the Stability of Subtilisin; P.N. Bryan. Increased Stability of Mutant Forms of Yeast Cyhrome c; D.R. Hickey, et al. Introduction to Formulation of Protein Pharmaceuticals; M.A. Hanson, S.K.E. Rouan. PEG Modified Proteins; G.E. Francis, et al. Stabilization of Protein Structure by Solvent Additives; S.N. Timasheff. Heat-Shock Proteins and their Potential Uses for Pharmaceutical Protein Production in Microorganisms; J.M. McCoy. Index.

Editorial Reviews

‘Offers the most comprehensive treatment to date of the various degradation pathways of pharmaceutical proteins....The two-volume set is an essential reference for pharmaceutical scientists.'
BioPharm

From the Publisher

See preceding entry. Part B begins with degradation pathways that occur in vivo--of major concern during protein synthesis in cells, during their isolation and purification, and during their use in organisms. Finally, the volume includes a discussion of methods designed to enhance protein stability in order to obtain a more useful and beneficial therapeutic agent. The techniques include altering the primary structure of the protein through site-directed mutagenesis to produce a more stable protein entity. Stabilization attained through proper formulation of the protein or by a variety of chemical modifications is described in detail as well. Annotation c. Book News, Inc., Portland, OR (booknews.com)

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