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1 column, and the crystallins were tested for argpyrimidine.
2 mpared the concentrations of pentosidine and argpyrimidine.
3 dditional evidence that human lenses contain argpyrimidine.
4 R103 in alphaA-crystallin were converted to argpyrimidine.
5 ted to HPLC, and the eluate was analyzed for argpyrimidine.
6 tion between MG and arginine, which we named argpyrimidine.
7 To determine whether the human lens contains argpyrimidine, a modification of arginine by methylglyox
8 recipitation or with immunoaffinity-purified argpyrimidine-alpha-crystallin indicates that 50-60% of
9 The antibody recognized imidazolysine and argpyrimidine and a glyoxal-derived lysine-lysine cross-
12 Fluorescence of Trp, its derivatives and argpyrimidine (ArgP) can be excited at the red edge of t
13 xycarbonylarginine and MG, and we identified argpyrimidine as one of the epitopes from this incubatio
14 enomenon which we attributed to formation of argpyrimidine at arginine residues (R) 21, 49, and 103.
15 ight aggregates reacted with the antibody to argpyrimidine, but a protein of approximately 28 kDa in
16 A monoclonal antibody was used to measure argpyrimidine by a competitive ELISA in water soluble (W
17 ze tissue proteins with 6 N HCl and quantify argpyrimidine by high-performance liquid chromatography.
21 serum and lens proteins were much lower than argpyrimidine concentrations; in general, argpyrimidine
22 arginine by methylglyoxal, to establish how argpyrimidine content relates to lens aging and cataract
24 tive ELISA showed two to three times as much argpyrimidine in water-insoluble proteins as in water-so
25 e insoluble protein fractions was found, the argpyrimidine levels in brunescent cataractous lenses we
26 an argpyrimidine concentrations; in general, argpyrimidine levels were 10--25 times higher than pento
28 otal modification) with a minor formation of argpyrimidine, N(epsilon)-(1-carboxyethyl)lysine, and me
29 s than those from noncataractous lenses, and argpyrimidine was found in both crystallin monomers and
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