Publisher Summary Lectins play an important role in the development of immunology. Lectins also find application in serological laboratories for typing blood and determining secretor status, separating leucocytes from erythrocytes, and agglutinating cells from blood in the preparation of plasma. They serve as reagents for the detection, isolation, and characterization of carbohydrate-containing macromolecules, including blood-group antigens. In their interaction with saccharides, lectins serve as models for carbohydrate-specific antibodies, with the important advantage to purify lectins in gram quantities. Lectins are classified according to their carbohydrate-binding specificity that includes D-mannose(D-glucose)-binding lectins and 2-acetamido-2-deoxy-D-glucose-binding lectins. The chapter considers only those lectins that have been purified to homogeneity, and studied with regard to their biophysical, biochemical, and carbohydrate-binding specificity. The chapter also describes the cell-binding and biological properties of lectins. The chapter concludes with the description of several glycopeptide structures showing the carbohydrate-binding loci with which various lectins interact.

The lectins : carbohydrate-binding proteins of plants and animals

Recombinant DNA technology has now made it possible to produce proteins for pharmaceutical applications Consequently, proteins produced via biotechnology now comprise a significant portion of the drugs currently under development Isolation, purification, formulation, and delivery of proteins represent significant challenges to pharmaceutical scientists, as proteins possess unique chemical and physical properties These properties pose difficult stability problems A summary of both chemical and physical decomposition pathways for proteins is given Chemical instability can include proteolysis, deamidation, oxidation, racemization, and β-elimination Physical instability refers to processes such as aggregation, precipitation, denaturation, and adsorption to surfaces Current methodology to stabilize proteins is presented, including additives, excipients, chemical modification, and the use of site-directed mutagenesis to produce a more stable protein species

Stability of Protein Pharmaceuticals

Proteins for foods, in addition to providing nutrition, should also possess specific functional properties that facilitate processing and serve as the basis of product performance. Functional properties of proteins for foods connote the physicochemical properties which govern the behavior of protein in foods. This general article collates the published information concerning the major functional properties of food proteins, e.g., solubility, binding properties, surfactant properties, viscogenic texturizing characteristics, etc. The effects of extraction and processing on functional properties and possible correlations between structure and function are discussed, in relation to practical performance in food systems. Modification of proteins to improve functional characteristics is briefly mentioned.

Functional properties of proteins in foods: A survey

A brief survey of methods for preparing protein conjugates with dyes, haptens, and cross-linking reagents.

O-linked oligosaccharides of mouse egg ZP3 account for its sperm receptor activity

Effects of alkali on proteins. Disulfides and their products.

Antifreeze glycoproteins from the blood of an antarctic fish. The structure of the proline-containing glycopeptides.

Amine boranes as alternative reducing agents for reductive alkylation of proteins.

http://www.jbc.org/content/247/24/7885.full.pdf

Ahmed I. Ahmed

Papers

Effects of alkali on proteins. Disulfides and their products.

Antifreeze glycoproteins from the blood of an antarctic fish. The structure of the proline-containing glycopeptides.

Amine boranes as alternative reducing agents for reductive alkylation of proteins.

Structure and Role of Carbohydrate in Freezing Point-depressing Glycoproteins from an Antarctic Fish

Antifreeze glycoproteins from an Antarctic fish. Quasi-elastic light scattering studies of the hydrodynamic conformations of antifreeze glycoproteins.