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The third component of complement, C3, is one of the most versatile proteins and an important participant in immune surveillance and immune response pathways. Its multifunctio nality is based on its ability to interact specifically with multiple serum complement proteins, cell surface receptors, and mem brant;-associated regulatory proteins. One of its most intriguing strategies of interaction with cell surfaces is the covalent binding of activated C3 through the internal thioester. The field has expanded over the past 10 years and a wealth of information has accumulated. C3 from various species and many of the human C3 binding proteins have been cloned and expressed. Numerous cellular responses mediated by the diffe rent fragments of C3 have been described. The findings that C3 interacts in a ligand-receptor-like fashion with proteins of nonself origin such as the gC of herpes simplex virus, a 70-kDa protein from Candida albicans, proteins from Epstein-Barr virus, etc. has opened a new field of investigation. The papers assembled in this volume summarize the wealth of data on the various aspects of the C3 interactions; together they bring to the reader new information on the chemistry, molecular gene tics, biology, and pathophysiology of C3 and C3-binding proteins. Emphasis is given to structural features as they relate to functions. Spring 1989 JOHN D. LAMBRIS, HANS J. MULLER-EBERHARD Table of Contents J. E. VOLANAKIS: Participation of C3 and Its Ligands in Complement Activation . . . . . . . . . . . 1 S. R. BARNUM, G. FEY, and B. F. TACK: Biosynthesis and Genetics of C3 . . . . . . . . . . . . .
This book provides comprehensive up-to-date information on the structure and function of immunoglobulins. It describes the basic features of these molecules, which assists the reader in understanding how they function as an integral part of the immune system. The Immunoglobulins describes the localization and structure of different binding sites of immunoglobulin molecules, including the antigen-binding site, on the basis of latest x-ray crystallography studies. It discusses recently developed biotechnological methods that allow scientists to obtain fully active antibody molecules in vitro even without immunization and to construct new variants of immunoglobulins and their fragments by fusing with various other active molecules. A survey of recent knowledge on immunoglobulin-binding molecules other than antigens and on flexibility of immunoglobulin molecules concludes the discussion of functional aspects of the problem. - Describes recent reviews on the structure and function of immunoglobulin molecules of various species - Summarizes in detail recent findings on the fine structure of the antigen-combining site - Presents comparative data on the antigen-recognizing sites of other molecules such as MHC proteins and T-cell receptors - Summarizes growing data on immunoglobulin binding sites responsible for the reaction of immunoglobulins with molecules other than antigens - Explores the rapid advance of recent biotechnological methods used for the construction of antibody molecules and their fragments with new properties - Presents extensive references and is lavishly illustrated
The complement system is a protein system that combines with antibodies to form a defense against bugs and viruses. This book contains entries on all its components, including C1q and lectins, serine proteases, and terminal pathway proteins.
Consists chiefly of reprints from various medical journals.