FEBS Letters | |
Muramyl peptides bind specifically to rat brain membranes | |
Tsetlin, V.I.1  Kaydalov, A.A.1  Utkin, Yu.N.1  Andronova, T.M.1  Ivanov, V.T.1  | |
[1] Shemyakin Institute of Bioorganic Chemistry, USSR Academy of Sciences, Moscow V-437, USSR | |
关键词: Muramyl peptide; Specific binding; (Rat brain); Azs; 4-azidosalicyl; BSA; bovine serum albumin; GMDP; N-acetylglucosaminylmuramyl dipeptide; GMDP-Lys; GMDP-Lys(Azs) and GMDP-Lys(Hp); GMDP analogs with free or acylated lysine side chain; Hp; 3-(4-hydroxyphenyl)propionyl; MDP; muramyl dipeptide; Taps; N-tris(hydroxymethyl)-3-aminopropanesulfonic acid; | |
DOI : 10.1016/0014-5793(89)80435-1 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
The capability of immunoactive muramyl peptides to bind specifically to rat brain membranes has been discovered. The reaction of an N-acetylglucosaminylmuramyl dipeptide analog having an additional C-terminal lysine residue (GMDP-Lys) with Bolton-Hunter reagent or N-hydroxysuccinimidyl-4-azidosalicylate afforded two acylated derivatives, GMDP-Lys-(Hp) and GMDP-Lys(Azs). Their iodination resulted in radioactive derivatives (spec. act. ∼2000 Ci/mmol) whose binding to rat brain membranes is characterized by K d∼3 nM and B max∼10 fmol/mg membrane protein. Binding could be inhibited by muramyl dipeptide (MDP), GMDP-Lys, and GMDP, while fragments of the latter, N-acetylglucosamine, dipeptide and disaccharide, were ineffective.
【 授权许可】
Unknown
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