A practical guide to protein and peptide purification for microsequencing

A practical guide to protein and peptide purification for microsequencing

T I B T E C H - J U L Y 1990 [Vol. 8] 195 and concluding with detailed outlines of a number of such syntheses. This to me is the most important part...

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T I B T E C H - J U L Y 1990 [Vol. 8]

195

and concluding with detailed outlines of a number of such syntheses. This to me is the most important part of the book, and it is disappointingly brief. Some form of compilation of awkward couplings and difficult residues would have been very useful. The examples in the final chapter were chosen because they had 'sequence features which caused concern', but it is not immediately []

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obvious to the novice what constitute awkward, or potentially awkward, peptides, and some prior warning of where problems are liable to occur would have been helpful. This is an excellent book for anyone considering peptide synthesis, and a most useful reference for anyone currently using the FMOC polyamide approach. The authors have []

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Preparing proteins for sequence analysis A P R A C T I C A L GUIDE T O PROTEIN A N D PEPTIDE P U R I F I C A T I O N FOR MICROSEQUENCING

edited by P. Matsudaira, Academic Press, 1989. US $24.95 (xi + 131 pages) ISBN 0 12 480280 X The practical guide results from the collation and editing of protocols supplied by participants at the joint meeting of the American Societies of Cell Biology and Molecular Biology and Biochemistry in 1989. It is a budget priced, spiral bound volume and the recipes are reasonably clear and easy to read. The introduction is philosophical strategies for isolating single components from protein mixtures and fragmenting the protein of interest for sequence analysis. Of these strategies, the electrophoretic isolation of proteins is fully described and fragmentation by proteases is dealt with to a limited extent (trypsin, endoprotease Lys-C and ~-chymo-trypsin). -

The major techniques of liquid chromatographic separation (with the exception of peptide isolation by reverse-phase HPLC) are not described. The final chapter deals with MS/MS for obtaining amino acid sequence information (really a brief guide to mass spectral interpretation). The introduction also contains sensible and helpful hints and tips for people with a gas phase sequencer; these are very useful and give full references, which are organized in the form of a bibliography with subject headings. There have been many books published in the last two years that cover essentially the same ground, from full, detailed (and frequently repetitive) multi-authored works, to monographs. The strength of this book really lies in its comprehensive coverage of electrophoretic methods for protein isolation for amino acid sequencing purposes. The focus of

succeeded in providing a readable summary of the topic, and the book does indeed contain much valuable practical information. G R A H A M KEMP

Department of Biochemistry and Microbiology, University of St Andrews, St Andrews KY16 9AL, UK. []

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attention is on electroblotting of PAGE-separated proteins, which reflects the skills and research interests of the editor, Paul Matsudaira. Hence, electrophoresis, blotting onto a variety of matrices, elution, fragmentation, peptide separation and amino acid composition analysis of electroblotted proteins are all well described. A particularly helpful section gives a 'trouble-shooting guide' for problems in electrophoresis, blotting and subsequent sequence analysis of proteins. In summary, this is an excellent and valuable guide for those who wish to isolate samples for sequence analysis by electrophoretic techniques. Those who want a more general treatment of protein and peptide isolation and sequencing strategies will find better coverage elsewhere. MICHAEL GEISOW

Delta Biotechnology, Castle Court, Castle Boulevard, Nottingham NG7 1FS, UK.