Synthesis and catalytic activity of poly-L-histidyl-L-aspartyl-L-seryl-glycine
β Scribed by A. N. Sarwal; E. O. Adigun; R. A. Stephani; A. Kapoor
- Publisher
- John Wiley and Sons
- Year
- 1982
- Tongue
- English
- Weight
- 483 KB
- Volume
- 71
- Category
- Article
- ISSN
- 0022-3549
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β¦ Synopsis
Poly(His-Asp-Ser-Gly) was synthesized from the fully protected tetrapeptide active ester hydrochloride, which was prepared by stepwise coupling, using pentachlorophenyl ester and mixed anhydride methods. Complete deprotection of the protected tetrapeptide polymer was achieved by using 90% trifluoroacetic acid. The free polymer was dialyzed for 24 hr using a membrane (which retains molecules with molecular weights >5000). The catalytic activity wits determined by studying the hydrolysis of p-nitrophenyl acetate in 0.2 M phosphate buffer (pH 7.4) at 37". The catalytic coefficient of the dialyzed polymer was found to be 138 liters/mole/min.
π SIMILAR VOLUMES
The syntheses of the polypeptides poly(L-phenylalanyl-L-glutamyl-L-valyldycyl)glycine methyl ester and ply(L-phenylalanyl-~-~spartyl-~-valylglycyl)glycine methyl ester are described
## Abstract An efficient synthesis of the backbone modified glutathione analogue Ξ³β(LβΞ³βoxaglutamyl)βLβcysteinylβglycine (7), characterized by the presence of an urethane OβCOβNH linkage replacing the Ξ³βglutamylic CH~2~COβNH fragment is described. The new analogue has been fully characterized by ^1