Evaluation Of Cyanogen As A Conformational Probe For The Protein Human Serum Albumin

Techniques in Protein Chemistry VI, an invaluable bench-top reference source for protein chemists, highlights current methods in the following areas: Protein sequencing and amino acid analysis Mass spectral analysis of peptides and proteins Posttranslational processing High-sensitivity protein and peptide separations Protein folding and NMR Analysis of protein interactions Protein design and engineering Techniques in Protein Chemistry VI, an invaluable bench-top reference source for protein chemists, highlights current methods in the following areas: Protein sequencing and amino acid analysis Mass spectral analysis of peptides and proteins Posttranslational processing High-sensitivity protein and peptide separations Protein folding and NMR Analysis of protein interactions Protein design and engineering

The first of its kind, All About Albumin summarizes the chemistry, genetics, metabolism, clinical implications, and commercial aspects of albumin. It provides the most up-to-date sequences, structures, and compositions of many species, and includes more than 2000 references. Includes up-to-date sequences, structures, and compositions of many species Reviews the protein chemistry, genetic control, and metabolism of albumin Covers medical and cell culture applications in vivo and in vitro, with a section on handling albumin in the laboratory Presents the relationship of albumin to its superfamily with an updated scheme for their evolution First complete coverage of all aspects of serum albumin in one volume, with more than 2000 references

Food proteins constitute a diverse and complex collection of biological macro molecules. Although contributing to the nutritional quality of the foods we con sume, proteins also act as integral components by virtue of their diverse functional properties. The expression of these functional properties during the preparation, processing and storage of foods is largely dictated by changes to the structure or structure-related properties of the proteins involved. Therefore, germane to the optimal use of existing and future food protein sources is a thorough understanding of the nature of the relationships between structure and function. It is the goal of this book to aid in better defining these relationships. Two distinct sections are apparent: firstly, those chapters which address struc ture-function relationships using a variety of food systems as examples to demonstrate the intricacies of this relationship, and secondly, those chapters which discuss techniques used to either examine structural parameters or aid in establishing quantitative relationships between protein structure and function. The editors would like to thank all contributors for their assistance, co-operation and, above all, their patience in putting this volume together, and the following companies/organizations for their financial support without which it would not have been the success it was: Ault Foods Limited, Best Foods Canada Limited, Natural Sciences and Engineering Research Council of Canada, Ontario Ministry of Agriculture and Food, Quest International Canada Inc., and University of Guelph. R.Y.Y. R.LJ.

Monthly, with annual cumulation. Recurring bibliography from MEDLARS data base. Index medicus format. Entries arranged under subject, review, and author sections. Subject, author indexes.

This book presents a comprehensive overview of medical and pharmaceutical applications of human serum albumin (HSA), with updates on structural aspects of albumin from the perspectives of X-ray crystallography and NMR, endogenous and exogenous ligand binding of albumin in various pathological conditions, and genetic variants and their phenotypes. Rapid progress and development of its applications have resulted in outstanding results for which albumin has clearly been proven to be a robust biomaterial. Contributions from leading international experts in this field show how HSA is applied to diagnosis, therapy, drugs, and treatment, with a comprehensive introduction of HSA. This volume will appeal to scientists in pharmaceutical and medical research including pharmaceutical chemists, pharmacokineticists, toxicologists, and biochemists not only in academia but also in industry. Readers can effectively acquire the most recent knowledge of applications of HSA and its impact on human health in a single volume.

Albumin Structure, Function and Uses reviews the many facets of serum albumin, including its history and evolutionary development, structure and function, synthesis, degradation, distribution and transport, and metabolic behavior. The use, misuse, and abuse of albumin in the treatment of disease are also discussed. This book is comprised of 17 chapters and begins with a commentary on how albumin is used, misused, and abused in the treatment of disease such as peptic ulcer, and a description of the real indications for its use. Concepts in albumin purification are then examined, along with the amino acid sequence of serum albumin and some aspects of its structure and conformational properties. Subsequent chapters explore the phylogenetics of albumin; albumin binding sites; clinical implications of drug-albumin interaction; genetics of human serum albumin; and hepatic synthesis of export proteins. Albumin catabolism and intracellular transport are also considered, together with surgical and clinical aspects of albumin metabolism. This monograph should be a useful resource for biochemists and clinicians.

Metalloproteins comprise approximately 30% of all known proteins, and are involved in a variety of biologically important processes, including oxygen transport, biosynthesis, electron transfer, biodegradation, drug metabolism, proteolysis, and hydrolysis of amides and esters, environmental sulfur and nitrogen cycles, and disease mechanisms. EPR spectroscopy has an important role in not only the geometric structural characterization of the redox cofactors in metalloproteins but also their electronic structure, as this is crucial for their reactivity. The advent of x-ray crystallographic snapshots of the active site redox cofactors in metalloenzymes in conjunction with high-resolution EPR spectroscopy has provided detailed structural insights into their catalytic mechanisms. This volume was conceived in 2005 at the Rocky Mountain Conference on Analytical Chemistry (EPR Symposium) to highlight the importance of high-resolution EPR spectroscopy to the structural (geometric and electronic) characterization of redox active cofactors in metalloproteins. We have been fortunate to have enlisted internationally recognized experts in this joint venture to provide the scientific community with an overview of high-resolution EPR and its application to metals in biology. This volume, High-Resolution EPR: Applications to Metalloenzymes and Metals in Medicine, covers high-resolution EPR methods, iron proteins, nickel and copper enzymes, and metals in medicine. An eloquent synopsis of each chapter is provided by John Pilbrow in the Introduction. A second volume, Metals in Biology: Applications of High-Resolution EPR to Metalloenzymes, will appear later this year covering the complement of other metalloproteins. One of the pioneers in the development of pulsed EPR and its application to metalloproteins was Arthur Schweiger, whose contribution we include in this volume. Unfortunately, he passed away suddenly during the preparation of this volume. The editors and coauthors are extremely honored to dedicate this volume to the memory of Arthur Schweiger in recognition of his technical advances and insights into pulsed EPR and its application to metalloproteins. Arthur was extremely humble and treated everyone with equal respect. He was a gifted educator with an ability to explain complex phenomena in terms of simple intuitive pictures, had a delightful personality, and continues to be sadly missed by the community. It is an honor for the editors to facilitate the dissemination of these excellent contributions to the scientific community. Suggestions for future volumes are always appreciated.