Amino Acid Analysis (AAA) is an integral part of analytical biochemistry. In a relatively short time, the variety of AAA methods has evolved dramatically with more methods shifting to the use of mass spectrometry (MS) as a detection method. Another new aspect is miniaturization. However, most importantly, AAA in this day and age should be viewed in the context of Metabolomics as a part of Systems Biology. Amino Acid Analysis: Methods and Protocols presents a broad spectrum of all available methods allowing for readers to choose the method that most suits their particular laboratory set-up and analytical needs. In this volume, a reader can find chapters describing general as well as specific approaches to the sample preparation. A number of chapters describe specific applications of AAA in clinical chemistry as well as in food analysis, microbiology, marine biology, drug metabolism, even archeology. Separate chapters are devoted to the application of AAA for protein quantitation and chiral AAA. Written in the highly successful Methods in Molecular BiologyTM series format, chapters contain introductions to their respective topics, lists of the necessary materials and reagents, step-by-step, readily reproducible laboratory protocols, and notes on troubleshooting and avoiding known pitfalls. Authoritative and accessible, Amino Acid Analysis: Methods and Protocols provides crucial techniques that can be applied across multiple disciplines by anyone involved in biomedical research or life sciences.

A collection of classic and cutting-edge techniques of high utility in answering specific biological questions about amino acids. Common methods include those based on HPLC or gas chromatography separation and analysis after precolumn derivatization. New techniques based on capillary electrophoresis separation, high-performance anion exchange chromatography, and mass spectrometry are also presented. Each method is described in step-by-step detail to ensure successful experimental results and emphasizes sample preparation, particularly the collection and storage of bodily fluids. Up-to-date and highly practical, Amino Acid Analysis Protocols offers analytical and clinical chemists, as well as a broad range of biological and biomedical investigators, a rich compendium of laboratory tools for the productive analysis of both common and uncommon amino acids.

"Protein Structure Analysis - Preparation and Characterization" is a compilation of practical approaches to the structural analysis of proteins and peptides. Here, about 20 authors describe and comment on techniques for sensitive protein purification and analysis. These methods are used worldwide in biochemical and biotechnical research currently being carried out in pharmaceu tical and biomedical laboratories or protein sequencing facilities. The chapters have been written by scientists with extensive ex perience in these fields, and the practical parts are well documen ted so that the reader should be able to easily reproduce the described techniques. The methods compiled in this book were demonstrated in student courses and in the EMBO Practical Course on "Microsequence Analysis of Proteins" held in Berlin September 10-15, 1995. The topics also derived from a FEBS Workshop, held in Halkidiki, Thessaloniki, Greece, in April, 1995. Most of the authors participated in these courses as lecturers and tutors and made these courses extremely lively and successful. Since polypeptides greatly vary depending on their specific structure and function, strategies for their structural analysis must for the most part be adapted to each individual protein. Therefore, advantages and limitations of the experimen tal approaches are discussed here critically, so that the reader becomes familiar with problems that might be encountered.

Techniques in Protein Chemistry III compiles papers presented at the Fifth Protein Society Symposium in Baltimore on June 22-26, 1991. This book discusses the protein and peptide recovery from PVDF membranes; high-sensitivity peptide mapping utilizing reversed-phase microbore and microcolumn liquid chromatography; and capillary electrophoresis for preparation of peptides and direct determination of amino acids. The TFMSA/TFA cleavage in t-Boc peptide synthesis; applications of automatic PTC amino acid analysis; and identification of O-glycosylation sites with a gas phase sequencer are also elaborated. This text likewise covers the conformational stability of the molten globule of cytochrome c and role of aqueous solvation in protein folding. This publication is useful to students and researchers interested in methods and research approaches on protein chemistry.

The First International Symposium on the Interface between Analytical Chemistry and Microbiology: Applications of Chromatography and Mass Spectrometry was held June 1987 at the University of South Carolina, Columbia, SC, U.S.A. The purpose of the "Interface" meeting was to forge connections between analytical chemists and microbiologists that are using chromatography and mass spectrometry to solve common problems. The goals were admirably fulfilled. Nearly a hundred participants from seven European countries, Japan, and the United States participated in hearing twenty-three plenary talks and thirty-six submitted papers and posters. The papers and discussions displayed the breadth and depth of current research applications and revealed future directions. This book "Analytical Microbiology Methods: Chromatography and Mass Spectrometry" is loosely based on some of the presentations and discussions at the meeting. Each chapter describes specific methodology and applications in the context of the relevant scientific background. The present book continues the theme of an earlier book, "Gas Chromatography/Mass Spectrometry Applications in Microbiology", edited by G. Odham, L. Larsson, and P-A. Mardh, published by Plenum Press in 1984.

This manual deals specifically with laboratory approaches to diagnosing inborn errors of metabolism. The key feature is that each chapter is sufficiently detailed so that any individual can adopt the described method into their own respective laboratory.