Roger L Lundblad

Chemical Reagents for Protein Modification

• Gebundenes Buch

Produktbeschreibung

A comprehensive review of reagents used for the chemical modification of proteins, the fourth edition represents a major revision. The completely updated text is substantially larger and includes five new chapters: Alkylating Agents, Acylating Agents, Nitration and Nitrosylation, Oxidation, and Modification of Proteins with Reducing Agents. The format has been markedly revised, presenting information based on the chemical nature of the modifying material and on the amino acid residue modified. Much of the information is in tabular form to enable the rapid location of cited material.

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Produktdetails

• Verlag: Taylor & Francis Ltd (Sales)
• 4th edition
• Seitenzahl: 684
• Erscheinungstermin: 22. Juli 2014
• Englisch
• Abmessung: 254mm x 180mm x 41mm
• Gewicht: 1315g
• ISBN-13: 9781466571907
• ISBN-10: 146657190X
• Artikelnr.: 40494364

Autorenporträt

Roger L. Lundblad is a native of San Francisco, California. He received his undergraduate education at Pacific Lutheran University and his PhD in biochemistry from the University of Washington. After his postdoctoral work in the laboratories of Stanford Moore and William Stein at The Rockefeller University, he joined the faculty of the University of North Carolina at Chapel Hill. He then joined the Hyland Division of Baxter Healthcare in 1990. Currently, Dr. Lundblad works as an independent consultant at Chapel Hill, North Carolina, and writes on biotechnological issues. He is an adjunct professor of pathology at the University of North Carolina at Chapel Hill.

Inhaltsangabe

Introduction to the Chemical Modification of Proteins. Alkylating Agents.
Acylating Agents. Nitration and Nitrosylation. Oxidation. Modification of
Proteins with Reducing Agents. Chemical Modification of Cysteine.
Modification of Sulfhydryl Groups in Proteins for Analysis. Conjugate
Nucleophilic Addition (Michael Addition). Alkyl Alkanethiosulfonates.
Chemical Modification of Cystine. Cleavage of Disulfide Bonds. Modification
of Methionine. Modification of Carboxyl Groups in Proteins. Modification of
Tyrosine Residues. Modification of Tryptophan. Modification of Amino
Groups. Modification of Histidine. Modification of Arginine. Index.