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Polymeric Proteins

Because of their functional importance, the gluten proteins have been studied in detail using genetical, molecular, biochemical, and biophysical approaches. This has revealed details of the numbers and locations of their controlling genes loci, their amino acid sequences, their conformations, and their relationship to various functional properties [39]. [Pg.389]

A wide range of approaches has been used to provide better purification of the glutenin fraction. After Osborne s studies, Jones et al. (1959) [46] tested two different methods (ethanol 70%, pH fractionation) for precipitating glutenin from gluten. [Pg.390]

The pioneer studies of Bietz and Wall (1972) showed that two t)q es of subunits were present, the low molecular weight (LMH-SG-10,000-70,000Da) and the high molecular glutenin subunits (HMW-SG-= 80,000-130,000Da) [47]. [Pg.390]

Little was known about the structure of these proteins until 20 years ago. Then, boosted by new technology developments such as molecular cloning, it became possible to isolate cloned cDNA and genes for all the major groups of gluten [Pg.391]


SARA is a scaffolding protein that regulates the subcellular localization of inactivated R-Smads, potentially scaffolding the TGF-P receptor kinase to the Smad 2 substrate. Filamins are a family of actin polymerization proteins that also form scaffolds for a range of signaling proteins including SAP kinases such as MKK-4, small GTPases Rho and Ras, as well as Smad 2 and Smad 5. [Pg.1230]

The use of stereochemical concepts for the description of the association of subunits in oligomeric and polymeric proteins has been discussed by Hanson 7>, who has provided a clarifying summary of terminology, as well as some interesting examples. [Pg.49]

The translation of the mRNA into proteins is the final step in the biological flow of information (see Fig. 6.1). Similar to other macromolecular polymerizations, protein synthesis can be divided into initiation, chain elongation, and termination. Critical players in this process are the aminoacyl transfer RNAs (tRNAs). These molecules form the interface between the mRNA and the growing polypeptide. Activation of tRNA involves the addition of an amino acid to its acceptor stem, a reaction catalyzed by an aminoacyl-tRNA synthetase. Each aminoacyl-tRNA synthetase is highly specific for one amino acid and its corresponding tRNA molecule. The anticodon loop of each aminoacyl-tRNA interacts... [Pg.71]

Lee KY, Yuk SH (2007) Polymeric protein delivery systems. Prog Polym Sci 32 669-697... [Pg.187]

Polymeric protein mixtures were prepared by Kornguth et al. [51] by cross-linking anti-human T cell antibodies, gelatin and bovine serum albumin with DTPA dianhydride. The Gd(III) chelates were prepared and the protein mixture was used to effectively image human T cell implants, 48 to 72 hours after injection, in the presence of bovine T cells that were not contrast enhanced. [Pg.136]

Thus, questions remain about the natural role of FFA as settlement inducers in Phragmatopoma lapidosa californica, and it is very likely that the FFA are another type of artificial inducer, such as cations, GABA, and organic solvents.8788 Additional research is warranted to resolve the roles of FFA and polymeric proteins containing l-DOPA residues in inducing settlement and metamorphosis of P. 1. californica and to determine whether either or both types of molecules are important in nature. [Pg.439]

Resolution is generally not quite so high as with STM. However, applications to some forms of polymerization, protein adsorption on insulating surfaces, and corrosion of anodic oxide films are made possible by this arrangement. [Pg.270]

The most widely accepted theory of prion diseases suggests that the infectious prion protein has the same primary structure as a normal protein found in nerve cells, but it differs in its tertiary structure. In effect, it is a misfolded, denatured version of a normal protein that polymerizes to form the amyloid protein plaques seen in the brains of infected animals. When an animal ingests infected food, the polymerized protein resists digestion. Because it is simply a misfolded version of a normal protein, the infectious prion does not provoke the host s immune system to attack the pathogen. [Pg.1194]

An alternative way of viewing the concept of extrinsic binding constants is as follows. The experimentally measured binding constant for each site of a polymeric protein, or enzyme, will depend on the number of available sites on each molecule e.g., for the hemoglobin tetramer the first binding reaction is... [Pg.269]

Fig. 6. Cyclization and polymerization of proteins. Two approaches that employ inteins for the generation of circular recombinant protein, split intein system (A), and TWIN system (B), are demonstrated. (A), The target protein is inserted between the C-terminal intein (C-intein) and the N-terminal intein (N-intein) segment. After spontaneous intein assembly, the standard splicing reaction results in excised intein and cyclized target protein. (B), The two intein systems sandwich the target protein between two intein-CBD tags. Controlled C- and N-terminal intein cleavages lead to target protein owning both N-terminal cysteine and C-terminal thioester. Whereas the intramolecular condensation forms cycUzed proteins, intermolecular reaction gives dimeric and polymeric proteins. Fig. 6. Cyclization and polymerization of proteins. Two approaches that employ inteins for the generation of circular recombinant protein, split intein system (A), and TWIN system (B), are demonstrated. (A), The target protein is inserted between the C-terminal intein (C-intein) and the N-terminal intein (N-intein) segment. After spontaneous intein assembly, the standard splicing reaction results in excised intein and cyclized target protein. (B), The two intein systems sandwich the target protein between two intein-CBD tags. Controlled C- and N-terminal intein cleavages lead to target protein owning both N-terminal cysteine and C-terminal thioester. Whereas the intramolecular condensation forms cycUzed proteins, intermolecular reaction gives dimeric and polymeric proteins.
On numerous occasions in immunochemical study the need arises to link proteins to particles, to polymerize proteins or to form covalent conjugates of proteins and smaUer peptides. The availability of reagents that are simple and effective while largely preserving the native antigenicity of... [Pg.159]

In addition to widespread applications in the held of polymer and material science or environmental research, AF4 can be used in bioanalytics, especially for the characterization of proteins, protein aggregates, polymeric proteins, cells, cell organelles, viruses, liposomes, and various other bioparticles and biopolymers. [Pg.198]


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Hydrophilicity or Hydrophobicity of Polymeric Materials and Their Behavior toward Protein Adsorption

Incorporation of Membrane Proteins into Polymeric Membranes

Liposomes, Polymeric-Protein Incorporation, 93-95 (

Microtubule protein polymerization

Polymeric Materials with Ionic Functional Groups and Their Protein Adsorptive Behavior

Polymeric proteins, genetic control

Polymeric surfaces protein adhesion

Polymeric wheat proteins

Polymerization of protein

Protein A naturally occurring polymeric

Protein A naturally occurring polymeric chain of L-amino acids linked together

Protein filaments and actin polymerization

Protein polymeric character

Protein polymeric gels

Protein structure actin polymerization

Protein-polymeric membrane

Proteins polymerization

Proteins polymerization

Synthesis peptide polymerization protein

Viscosity polymeric proteins

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