Lysine serum

Collagen, poly-L-lysine/serum proteins from cell culture medium Crosslinked polyacrylic acid/polyacrylamide multilayer films, PEG Coculture of rat adrenal medulla cells and mouse fibroblasts L929 Photopatteming of polyelectrolyte multilayer film 2009 [110]... 

Poly-L-lysine/serum proteins from cell culture medium PEG-DMA... 

Transamination is not restricted to a-amino groups. The 5-amino group of ornithine—but not the e-amino group of lysine—readily undergoes transamination. Serum levels of aminotransferases are elevated in some disease states (see Figure 7-11). 

SUGANO M, ISHIWAKI N, NAKASHIMA K (1984) Dietary protein-dependent modification of serum cholesterol level in rats significance of Arginine/lysine ratio. rinw Nutr Metab, 28 192-9. 

Proteins may be covalently attached to the latex particle by a reaction of the chloromethyl group with a-amino groups of lysine residues. We studied this process (17) using bovine serum albumin as a model protein - the reaction is of considerable interest because latex-bound antigens or antibodies may be used for highly sensitive immunoassays. The temperature dependence of the rate of protein attachment to the latex particle was unusually small - this rate increased only by 27% when the temperature was raised from 25°C to 35°C. This suggests that non-covalent protein adsorption on the polymer is rate determining. On the other hand. the rate of chloride release increases in this temperature interval by a factor of 17 and while the protein is bound to the latex particle by only 2 bonds at 25°C, 22 bonds are formed at 35°C. 

Liver toxicity, as evidenced by alterations in the incorporation of lysine into liver proteins, was observed in rats administered 192 mg lead/kg/day by gavage as lead acetate for 9 weeks (Barratt et al. 1989). No effects were observed at 21 mg lead/kg/day. However, the toxicological significance of this finding is not known because neither serum enzymes nor histopathological evaluations were performed. 

Positive ROA bands in the range 1297-1312 cm-1 are also characteristic of a-helix. These are observed at 1300 cm-1 in human serum albumin (Fig. 4) and at 1297 cm-1 in a-helical poly-L-lysine (Fig. 3). These additional bands appear to be associated with a-helix in a more hydrophobic environment (Barron etal., 2000). The striking absence of a positive ROA band in the range 1297-1312 cm-1 in a-helical poly-L-glutamic acid would then suggest that only the hydrated form of a-helix is present, possibly due to the shorter side chains relative to poly-L-lysine,... 

Mir MM, Fazili KM, Abul Qasim M. Chemical modification of buried lysine residues of bovine serum albumin and its influence on protein conformation and bilirubin binding. Biochim. Biophys. Acta 1992 1119 261-267. 

Biocytin is e-N-biotinyl-L-lysine, a derivative of D-biotin containing a lysine group coupled at its e-amino side chain to the valeric acid carboxylate. It is a naturally occurring complex of biotin that is typically found in serum and urine, and probably represents breakdown products of recycling biotinylated proteins. The enzyme biotinidase specifically cleaves the lysine residue and releases the biotin component from biocytin (Ebrahim and Dakshinamurti, 1986, 1987). 

The most common carrier proteins in use today are keyhole limpet hemocyanin (KLH MW 4.5 X 105 to 1.3 X 107), BSA (MW 67,000), aminoethylated (or cationized) BSA (cBSA), thyroglobulin (MW 660,000), ovalbumin (OVA MW 43,000), and various toxoid proteins, including tetanus toxoid and diphtheria toxoid. Other proteins occasionally used include myoglobin, rabbit serum albumin, immunoglobulin molecules (particularly IgG) from bovine or mouse sera, tuberculin purified protein derivative, and synthetic polypeptides such as poly-L-lysine and poly-L-glutamic acid. 

The chemical structure of 2,5-hexanedione suggested that it could react with lysine side-chain amino groups in proteins to form pyrroles (see Figure 2-7). In vitro experiments showed that this was, in fact, the case, and that the modified proteins can undergo secondary reactions to yield oxidized and polymeric products (DeCaprio et al. 1982 Graham et al. 1982). Oral administration of 2,5-hexanedione produced evidence that this process can take place in vivo as demonstrated by the detection of 2,5-dimethylpyrrole adducts in serum and axonal cytoskeletal proteins (DeCaprio and O Neill 1985). When a series of... 

Serum samples from some animals fed the four dietary regimens were pooled and subjected to fractionation of the lipoproteins by agarose column chromatography. The total amounts of lipoproteins found in the sera from the four groups (ug/ml) were casein, 904 soy protein, 807 casein/arginine, 1,130 and, soy/lysine, 672. 

Table I. Serum Lipids and Aortic Atherosclerosis in Rabbits fed Casein, Soy Protein, Casein Arginine, or Soy Lysine...

We have demonstrated that addition of lysine to soy protein causes a significant increase of serum cholesterol and development of atherosclerosis. Another approach to this question was to feed three proteins of animal origin that contained almost identical amounts of lysine but different amounts of arginine. We used fish protein (lysine, 6.81 arginine, 4.74 L/A ratio, 1.44), casein (lysine, 6.91 arginine, 3.65 L/A ratio, 1.89), and milk protein (lysine, 6.61 arginine, 2.71 L/A ratio, 2.44) (14). The proteins... 

Table VII. Serum Lipids and Atherosclerosis in Rabbits fed Three Animal Proteins with Different Lysine/Arginine Ratios...

Furthermore, addition of lysine to soy protein markedly increased the rate of lipid absorption and addition of arginine to casein slowed lipid absorption. The slowed absorption of lipids in animals fed soy protein is similar to that reported for soluble fibers such as pectin and guar gum that act to lower serum cholesterol concentrations in a number of animal species, including humans. 

J. E. Walker, Lysine Residue 199 of Human Serum Albumin Is Modified by Acetylsal-icyclic Acid , FEBS Lett. 1976, 66, 173 -175. 

Penicillins and cephalosporins bind irreversibly to serum albumin. It has been shown that drug-protein conjugates result from the aminolysis of the /3-lactam bond by the e-amino group of lysine residues in the protein (Fig. 5.1, Pathway e). The bound penicilloyl group appears to be the major antigenic determinant of penicillin allergy [145-148],... 

Similarly, chemical hydrolysis of a number of a-amino acyl prodrugs of metronidazole (8.100, R=H see Sect. 8.5.4) was compared to the serum-catalyzed reaction [135][136]. The amino acids used for esterification included alanine, glycine, isoleucine, leucine, lysine, phenylalanine, and valine. Under physiological conditions of pH and temperature, ty2 values for hydrolysis in human serum ranged from 4.5 min for the Phe ester to 96 h for the lie ester. A good linear relationship was established between the log of the rate constant of enzymatic hydrolysis and the log of the rate constant of HO-cata-... 

Figure 4.3. The chemical synthesis of naproxen-HSA. Naproxen is first converted to an ester and is then coupled to the free E-NH2 of the lysine residues in human serum albumin (HSA). NHS N-hydroxysuccinimide, DCC dicyclohexylcarbodiimide.

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