Protein cationized

Yang, Y.-B., Harrison, K., and Kindsvater, J., Characterization of a novel stationary phase derived from a hydrophilic polystyrene-based resin for protein cation-exchange high-performance liquid chromatography, /. Chromatogr. A, 723, 1, 1996. 

Actin comprises about 5-8% of the total protein of the neutrophil, and in resting cells about 50-70% of the actin pool exists as a monomer. This proportion of monomeric G-actin is far in excess of what would be predicted from the critical concentration for actin assembly in vitro. Thus, in vivo actin polymerisation and depolymerisation is regulated by the activities of a number of binding proteins, cations and other regulatory molecules, which are in turn regulated by the activation status of the cell. 

R. A., Horn, D.M., Fridriksson, E.K., Kelleher, N.L., Kruger, N.A., Lewis, M.A., Carpenter, B.K., McLafferty, F.W. Electron capture dissociation for structural characterization of multiply charged protein cations. Anal. Chem. 2000, 72, 563-73. [d] Zubarev, R.A., Haselmann, K.F., Budnik, B., Kjeldsen, F., Jensen, F. Account towards an understanding of the mechanism of electron-capture dissociation a historical perspective and modern ideas. Eur. J. Mass Spectrom. 2002, 8, 337-49. 

Cationized proteins + Cationized albumin AMT Blood to brain [49]... 

R. A. Zubarev, N. L. Kelleher, and F. W. McLafferty, Electron capture dissociation of multiply charged protein cations. A nonergodic process, J. Am. Chem. Soc., 120 (1998) 3265-3266. 

DEAE Alkyl ether Ethyl 2° amine Salt buffers AN, MeOH, H20 Proteins, cations... 

Transient intermediates arising by radical additions to the amide bond have been studied recently in an effort to explain the complex processes occurring in electron-capture dissociation of multiply charged peptide and protein cations [192]. The amino(hydroxy)methyl radical, HC(OH)NH2 (64), is a prototypical species that represents the simplest model for radical additions to peptide bonds. Radical 64 was generated from cation 64+ which in turn was prepared by... 

Redesign of Ca fMg Specificity. Proteins in the calmodulin superfamily (including troponin C, parvalbumin (PV) and oncomodulin (OM)) share similar overall structure and yet have different selectivity for Ca and Mg see Calcium-binding Proteins, Cation-activated Enzymes). For example, PV and OM have four helix-tum-helix domains, two of which contain mixed Ca /Mg sites and two Ca -specific sites. The mixed Ca /Mg sites have been converted to Ca -specific sites by replacing amino acids with the corresponding residues in the Ca -specific site. " ... 

Some interesting conductance studies of protein-nonaqueous solvent systems have been carried out. Greenberg and Larson (1935), for example, found that gelatin, casein, and edestin dissolved in glacial formic acid (D = 56.5 at 16°C) showed marked increases of conductivity over that of the solvent, whereas no conductivity increment was observed with the same proteins dissolved in glacial lactic or acetic (D = 6.15 at 20°C) acids. This is in accord with the conclusions reached in Section IV,B,1, that in solvents of low dielectric constant, ion-pairing (in these cases, of the protein cations to lactate and acetate counterions) is essentially complete. Con-... 

Wool, silk, hair Natural, hydrophilic Complex proteins Cationic... 

Renal tubular cells Endothelia Low molar mass proteins (cationic)... 

In Chapter 7, Florman and coauthors review the mechanisms of egg-regulated acrosome reactions of mammalian sperm. Among the aspects discussed are the nature of primary signal transducers and targets stimulated by binding of acrosome-intact sperm to receptors in the egg zona pellucida. In a detailed presentation, the potential roles of several sperm components including G proteins, cation channels, tyrosine kinases, calcium, and cellular pH are considered. 

Soy-Quat C. (Mt lnook] Cocodimo-nium hydroxypropyl hydrolyzed soy protein cationic subsundvi i ent, conditioner, moistuTizer for hair and skin care prods. 

Figure 7-2 Re-reduction of bacterial cytochrome c peroxidase. Yeast cytochrome c peroxidase is a monoheme enzyme which is oxidized by hydrogen peroxide to yield a ferryl iron and a protein cation radical. Two electrons are required for re-reduction. The two-domain cytochrome c peroxidases contain a peroxidatic (P) heme and an electron transfer (E) heme. The state shown is at the end of a catalytic cycle and contains two oxidizing equivalents, one on the P heme (as Fe(IV)) and one on the E heme (as Fe(III)). Re-reduction of the enzyme could proceed via (1) a successive pair of electron transfers at the E heme with the first of the electrons passing to the P heme, (2) two separate electron transfer routes, or (3) a single electron transfer route which diverges within the protein.

Extraction of muscle fibers with water or glycerol-water mixtures removes 20% of the muscle protein, consisting for the most part of the sarcoplasmic fraction (Szent-Gyorgyi, 1949). The concentration of actomyosin is thereby increased from a value of about 50% in the case of living muscle (Hasselbach and Schneider, 1951) to one of about 65%. Of the salts originally present, only a few cations, mostly potassium, remain behind as protein cations, and these are mostly replaced by sodium ions when the extracting solution is buffered with sodium salts (E. J. Harris, personal communication). 

---