Protamines properties

In 1899 Kossel isolated a similar substance from the protamine, clupeine, of herring milt, and since then E. Fischer and his pupils have obtained it from caseinogen, horn and other proteins. The preparation from horn, when racemised, corresponded in properties with the synthetical a-aminoisovalerianic acid. 

Changes in the number of free amino residues alter the modified proteins susceptibility to proteolysis. Albumin chlorination and /V-chloramine formation decreases susceptibility to trypsin digestion. Removing of chloramine residues by treatment with thiosulfate shows that chlorination alters albumin properties by a biphasic mode the reversible chlorination and removal of chloramine moieties markedly increases albumin susceptibility to proteolysis, whereas chlorination produces the irreversible loss of amino moieties and carbonyl group formation effects decrease in albumin susceptibility to trypsin digestion. The effect is related to the number of lost amino residues. A similar relationship was observed for IgG. Fibrinogen and protamine, on the other hand, did not show dependence between chlorination and proneness to trypsin proteolysis (06). 

Antimicrobial activity only the undissociated acid shows antimicrobial properties, the activity therefore depends on the pH of the medium. Optimum activity occurs at pH values below 4.5 at values above pH 5, benzoic acid is almost inactive. It has been reported that antimicrobial activity is enhanced by the addition of protamine, a basic protein. ... 

Early experiments showed that a transferrin-polycation complex transported bacterial DNA into cells [12]. Ions are taken up by cells as an iron-transferrin complex by receptor-mediated endocytosis. Protamine or poly-lysine ligated by disulfide bonds to transferring and mixed with a lu-ciferase-encoding plasmid may bind the DNA because of the cationic properties of the complex [12]. Subsequently, avian ery-throblasts and human K-562 cells were incubated with the transferrin-polycation peptide-DNA complex, and the complexes were recognized and transported into the cells by receptor-mediated endocytosis and taken up into endosome-Hke intracellular vesicles [12]. Treatment with chloroquine (an agent that affects the endosomal pH) enhanced the uptake considerably. In contrast to other transfection methods, the transfection of cells with transferrin-mediated endocytosis did not cause significant cell death, because of the physiologi-... 

Salmine Sulfate. A protamine found in the sperm of salmon. Contains arginine, proline, serine, glycine, valine, leucine, alanine, threonine, isoleucine, lysine, histidine, aspartic and glutamic acids. Mol wt 6000 to 7000. N about 25%. Prepn and properties Fisher, Scott, J. Pharmacol. Exp. Ther. 58, 78 (1936) Felix. Am. Sci. 43, 431 (1955) Callanan et al., J. Biol Chem 229, 279 (1957) Carroll er al, ibid. 234, 2314 (1959). Separation of components and amino add sequence of major component Ando, Watanabe, Ini. J, Protein Res. 1, 221 (1969). 

SORPTION PROPERTIES OF PROTAMINE SULFATE / CARBOXYMETHYLCELLULOSE LAYER-BY-LAYER FILMS... 

Proteins from marine sources show promise as functional ingredients in foods because they possess numerous important and unique properties such as film and foaming capacity, gel-forming ability, and antimicrobial activity (Table I). Some of the most prevalent marine proteins used in foods are collagen, gelatin, and albumin, all of which can be extracted from fish and seafood by-products. The protein protamine has also shown promise for use in the food industry as a natural antibacterial preservative. 

In addition to the fish proteins already mentioned there is a renewed interest in specific protein fractions that can be recovered from by-products, particularly in the viscera. One such example is the basic protein or protamines found in the milt of the male fish, which can contain as much as 65% arginine. The best sources are salmonids and herring, whereas ground fish such as cod are not found to contain protamines. The extreme basic character of protamines makes them interesting for several reasons. As they adhere to most other proteins less basic, they can enhance the functional properties of other food proteins (if all the lipids present in the milt are removed from the protein preparation to avoid off-flavor development in the finished products). But the most promising feature of basic proteins is their ability to prevent growth of microorganisms. 

Y. Matsumura, K. Yamada, M. Takahashi, Y. Kikuchi, T. Tsuchido. Properties of bacterial corrosion of stainless steel and its inhibition by Protamine coating. Biocontrol Science, Vol. 12, No. 1, pp. 21-29, 2007. 

Protamide LMFAB. See Lauramide DEA Protamide LNO. See Linoleamide DEA Protamide MEAA. See Acetamide MEA Protamide MRCA. See Myristamide DEA Protamide SA. See Stearamide DEA Protamide X-45-B. SeeCocamide DEA Protamine sulfate CAS 9009-65-8 53597-25-4 Synonyms Salmine sulfate Definition Mixt. of simple proteins obtained from the sperm or testes of certain species of fish has property of neutralizing heparin Toxicoiogy LD50 (IP, rat) 120 mg/kg, (IV, rat) 75 mg/kg, (subcut., mouse) 200 mg/kg poison by IP, IV, subcut. routes human systemic effects (anaphylaxis, blood pressure decrease, decreased urine vol.) TSCA listed Hazardous Decomp. Prods. Heated to decomp., emits very toxic fumes of NOx and SOx Uses Pharmaceuticals (parenterals, injectables)... 

Using a similar approach to the isolation of acetyl-CoA carboxylase phosphatase. Lent and Kim (70) isolated a cyclic AMP-independent protein kinase for acetyl-CoA carboxylase (Table IV). The properties of this cyclic AMP-independent protein kinase are different from those reported by Shiao et al. (105). The enzyme had a Km for acetyl-CoA carboxylase of 85 nAf and requires CoA for activity. The significance of this CoA requirement is further discussed in Section V,C. Phos-phorylase b and HMG-CoA reductase do not serve as substrates for this kinase however, protamine, casein, and histones are phosphorylated. The subunit molecular weight, as measured under denaturing conditions, was 160,000, which is similar to that reported by Shiao et al. (105). However, the CoA-requiring enzyme exists in multimers under nondenaturing conditions, with molecular weights between 700,000 and 2 x 10 . 

Isoelectric point,/ / the pH value of a solution at which the net charge on the dissolved ampholyte is zero, i.e. the sum of the cationic charges is equal to the sum of the anionic charges. The pi of electrolytes, e.g. amino acids, peptides or proteins, may lie in the range from pH 1 ( psin) to pH 11.8 (protamine), and is characteristic for each amphol e. Certain characteristic properties appear at the pi, e.g. a minimal solubility and viscosity. Electrophoretic methods of separation arc based on the differences in the pi of the individual components. The pi. can be determined either electrophoretically at various pH values or by electrofocusing on an ampholine pH adient. 

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