Proteins neutral

Immunogenicity. Many, if not most, therapeutic proteins are potentially immunogenic when administered to humans. The likelihood that non-human proteins (e.g. murine monoclonal antibodies Chapter 13) are immunogenic in humans is an obvious one. However, human proteins can also be potentially immunogenic, as discussed in Box 4.1. Antibodies raised in this way can bind the therapeutic protein, neutralizing its activity and/or affecting its serum half-life. 

For instance, denaturation and partial hydrolysis of proteins oppositely influence their incompatibility with other biopolymers (Tolstoguzov 1991). Most biopolymers are polyelectrolytes. Factors such as pH and salt concentration affect their interactions with one another, with the solvent and their compatibility. For instance, when the pH is shifted to their isoelectric point (lEP), the thermodynamic incompatibility of proteins is usually enhanced by self-association of the protein molecules. Generally, protein-neutral polysaccharide mixtures separate into two phases when the salt concentration exceeds 0.15 M. 

Sweet, S.M.M. Creese, A.J. Cooper, H.J. Strategy for the identification of sites of phosphorylation in proteins Neutral loss triggered electron capture dissociation. Anal. Chem. 2006, 78, 7563-7569. 

Figure 8.15. Stereo view of yeast cytochromes b and Cl of Complex III showing Qo and heme Ci binding sites for the FeS center of the Rieske Iron Protein. Neutral residues are given in light gray, aromatic residues in black, other hydrophobic residues in gray, and charged residues in white in order to show visually the relative hydrophobicity of the two sites. Note at the Qo site that ubiquinol would reside at the base of a hydrophobic pit into which the hydrophobic FeS tip of the Rieske Iron Protein fits (see Figure 8.16), whereas the heme Cj site is not as hydrophobic. Also note that the hydrophobic residues L263 and V264...

Enzymes can be used to help the starch hydrolysis (typically a-amylases), solve filtration problems caused by P-glucans present in malt (P-glucanases), hydrolyze proteins (neutral proteinase), and control haze during maturation, filtration, and storage (papain, a-amylase, and P-glucanase). 

OnGuard-A Strong basic anion exchanger in the bicarbonate form Removal of Anions, peptides, proteins, neutralization of addic solutions... 

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