protein blotting: methodology, research and diagnostic applications

1
TIBS15-JANUARY1990 B00KS in BRIEF ProteinBlotting:Methodology, Research and Diagnostic Applications edited by B.A. Baldo and £.R. Tovey, S. Karger, 1989. $74.75 (viii + 168 pages) ISBN3 8055 48818 The occurrence of the terms 'protein blotting' or 'western blotting' has increased dramatically in scientific publications as is pointed out in the introductory chapter of this book. Thus, a thorough text on these techniques is justified. The present attempt does not, however, deliver what the title could imply to some: anticipation of a 'blot- tologist's' handbook, which will not only address the old problems and provide solutions, but also introduce the reader to new scopes of this field. The review chapter by Garfin and Bets is quite extensive, yet cannot be used easily as a practical guide. The discussions on various aspects of blotting are informative and, despite the obvious biased tendency of the authors to exploit their chapter as advertisement for their company, the article is interesting and does provide a good general overview on protein blotting. The third chapter, by Tovey and Bafdo, is by far the most useful in the book. It is extremely well written and gives a comprehensive treatment of aspects of sequencing of blotted peptides and the utility of blots as antigens or as intermediates for purification of mono- specific antibodies. The four remaining chapters are detailed descriptions of specific applications of protein blotting which may not immediately be regarded as applicable to the general reader. Articles of broader discussion on generic applications might have been more helpful. In summary, whereas there is a substantial amount of useful information in this volume, it does not necessarily satisfy the expectations of the novice blotter and will be most appreciated by the more experienced, providing yet another view. J.G. ProteinFunction: A Practical Approach edited by T. E. Cmlghton, IRLPress, 1989. £29. O0 (xx + 306pages) ISBN 0 19 963006 2 This volume covers a wide range of methods for the determination of protein function. They range from common-sense advice on avoiding protein inactivation to efficient techniques for site-directed mutagenesis. In between, chapters deal with basic bio- chemical techniques for the determination of ligand-protein affinities and the role of subunits in protein function. Three chapters are devoted to procedures utilizing gel electrophoresis: in ligand blotting and in the analysis and purification of sequence- specific DNA-binding proteins. Classical approaches in protein chemistry are well represented with chapters on affinity label- ling, crosslinking, competitive labelling and chemical modification. In general, the techniques are introduced adequately with the practical details clearly laid out in separate sections thereby facilitating the transition from printed work to experiment. The index is thorough and the illustrations used are well laid out and informative. The content and references are up-to-date and the book represents good value for money for students and post-graduate scientists. Continuing in the mould of the Practical Approach series, this book should become a valuable source of useful information in many laboratories and departmental libraries. R.H. ProteinStructure: A PracticalApproach edited by 1". E. Ctelghton, IRLPress 1989. £20. O0 (pbk)/£30. O0 (hbk) (380 pages) ISBNO 19 963000 3 When thinking about the study of protein structure, one naturally thinks of high- powered and high-cost methods such as X-ray crystallography and NMR spectroscopy. By contrast, this excellent little book is concerned with techniques which require only the kind of equipment which will be available in almost any biochemical laboratory, but which nonetheless provide a good deal of information on the structure, conformation and stability of proteins. The versatility of simple gel electrophoresis, for example, is amply demonstrated by its appearance as the focus of four chapters, on isoelectric focusing, two- dimensional PAGE,molecular weight determination by SDS-PAGEand non- denaturing and transverse gradient gel electrophoresis; and in a major role in two more, on peptide mapping, and on methods for determination and location of disulphide bonds. The chapter by Goldenberg contains a particularly useful guide to urea gradient gel electrophoresis, a valuable and insufficiently used method. Other areas covered include the assessment of conformation by optical spectroscopy and by immunological methods and the immunochemical detection of proteins of known sequence. Argos provides a succinct guide to the comparison of, and prediction of structure from, amino acid sequences. Finally, there is a valuable group of three chapters on the folding, unfolding and stabilization of protein structure. This volume is not comprehensive, and clearly could not be, but the selection of topics is sensible (particularly bearing in mind the content of other volumes in the series). Almost any laboratory involved in the characterization of proteins will find something useful here. Each chapter follows in the tradition of this valuable series in providing the kind of practical detail and advice one needs to actually do the experiments. This is a book for the bench rather than the shelf, and the hardback spiral- bound version seems well suited for the continuous use it is likely to get. G.C.K.R. PI~ send boo ils or b o ~ to: 37

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TIBS 15-JANUARY1990

B00KS in BRIEF Protein Blotting: Methodology, Research and Diagnostic Applications

edited by B.A. Baldo and £.R. Tovey, S. Karger, 1989. $74.75 (viii + 168 pages) ISBN 3 8055 48818

The occurrence of the terms 'protein blotting' or 'western blotting' has increased dramatically in scientific publications as is pointed out in the introductory chapter of this book. Thus, a thorough text on these techniques is justified. The present attempt does not, however, deliver what the title could imply to some: anticipation of a 'blot-

tologist's' handbook, which will not only address the old problems and provide solutions, but also introduce the reader to new scopes of this field.

The review chapter by Garfin and Bets is quite extensive, yet cannot be used easily as a practical guide. The discussions on various aspects of blotting are informative and, despite the obvious biased tendency of the authors to exploit their chapter as advertisement for their company, the article is interesting and does provide a good general overview on protein blotting. The third chapter, by Tovey and Bafdo, is by far the most useful in the book. It is extremely well written and gives a comprehensive treatment of aspects of sequencing of blotted

peptides and the utility of blots as antigens or as intermediates for purification of mono- specific antibodies. The four remaining chapters are detailed descriptions of specific applications of protein blotting which may not immediately be regarded as applicable to the general reader. Articles of broader discussion on generic applications might have been more helpful.

In summary, whereas there is a substantial amount of useful information in this volume, it does not necessarily satisfy the expectations of the novice blotter and will be most appreciated by the more experienced, providing yet another view.

J.G.

Protein Function: A Practical Approach

edited by T. E. Cmlghton, IRL Press, 1989. £29. O0 (xx + 306pages) ISBN 0 19 963006 2

This volume covers a wide range of methods for the determination of protein function. They range from common-sense advice on avoiding protein inactivation to efficient techniques for site-directed mutagenesis. In between, chapters deal with basic bio-

chemical techniques for the determination of ligand-protein affinities and the role of subunits in protein function. Three chapters are devoted to procedures utilizing gel electrophoresis: in ligand blotting and in the analysis and purification of sequence- specific DNA-binding proteins. Classical approaches in protein chemistry are well represented with chapters on affinity label- ling, crosslinking, competitive labelling and chemical modification. In general, the techniques are introduced adequately with the practical details clearly laid out in

separate sections thereby facilitating the transition from printed work to experiment.

The index is thorough and the illustrations used are well laid out and informative. The content and references are up-to-date and the book represents good value for money for students and post-graduate scientists. Continuing in the mould of the Practical Approach series, this book should become a valuable source of useful information in many laboratories and departmental libraries. R.H.

Protein Structure: A Practical Approach

edited by 1". E. Ctelghton, IRL Press 1989. £20. O0 (pbk)/£30. O0 (hbk) (380 pages) ISBNO 19 963000 3

When thinking about the study of protein structure, one naturally thinks of high- powered and high-cost methods such as X-ray crystallography and NMR spectroscopy. By contrast, this excellent little book is concerned with techniques which require only the kind of equipment which will be available in almost any biochemical laboratory, but which nonetheless provide a good deal of information on the structure, conformation and stability of proteins.

The versatility of simple gel electrophoresis, for example, is amply demonstrated by its appearance as the focus of four chapters, on isoelectric focusing, two- dimensional PAGE, molecular weight determination by SDS-PAGE and non- denaturing and transverse gradient gel electrophoresis; and in a major role in two more, on peptide mapping, and on methods

for determination and location of disulphide bonds. The chapter by Goldenberg contains a particularly useful guide to urea gradient gel electrophoresis, a valuable and insufficiently used method. Other areas covered include the assessment of conformation by optical spectroscopy and by immunological methods and the immunochemical detection of proteins of known sequence. Argos provides a succinct guide to the comparison of, and prediction of structure from, amino acid sequences. Finally, there is a valuable group of three chapters on the folding, unfolding and stabilization of protein structure.

This volume is not comprehensive, and clearly could not be, but the selection of topics is sensible (particularly bearing in mind the content of other volumes in the series). Almost any laboratory involved in the characterization of proteins will find something useful here. Each chapter follows in the tradition of this valuable series in providing the kind of practical detail and advice one needs to actually do the experiments. This is a book for the bench rather than the shelf, and the hardback spiral- bound version seems well suited for the continuous use it is likely to get. G.C.K.R.

P I ~ send boo ils or b o ~ to:

37