Plasma protein binding characteristics of decapeptide in several species / 中国药学杂志

OBJECTIVE: To study the plasma protein binding rate of decapeptide in several species. METHODS: Ultrafiltration was employed to separate the free and bound decapeptide, acetonitrile was used to precipitate protein, then the plasma concentration of decapeptide by HPLC-MS/MS. RESULTS: The plasma protein binding rates of decapeptide at low, middle and high concentrations (50.0, 100.0, and 800.0 ng·mL-1) were (95.9±1.1)%, (97.40±0.7)% and (94.9±0.6)% in SD rats,(96.8±0.8)%, (97.8±0.2)% and (96.9±0.5)% in Beagle dogs, and (97.3±1.0)%, (98.6±0.2 )% and (96.2±0.9)% in humans, respectively. The average plasma protein binding rate was 96.2% after subcutaneous administration at 200 μg·kg-1 in SD rats. And the average plasma protein binding rate was 97.1% after intramuscular injection at 320 μg·kg-1 in Beagle dogs. CONCLUSION: Decapeptide has potent binding ability to plasma protein in several species. The plasma protein binding rate of decapeptide is independent of its plasma concentrations.

A monoclonal antibody 1F9 against Torpedo Acetylcholinesterase recognizes specifically an antigenic epitope of the human brain Acetylcholinesterase / 中国免疫学杂志

Objective:In order to research the relationship between the function and the structure of human brain Acetylcholinesterase,use the monocolonal antibodies scanning antigenic decapeptides of human brain Acetylcholinesterase.Methods:Synthesis of overlapping decapeptides corresponding to the sequence of the human brain Acetylcholinesterase has been carried out on biotinylated with primary amino groups according to a method developed by M Geyson. Peptides Synthesized using the multipincombinatorial chemical synthesis technique have been used in an enzyme linked immunoabsorbent assay.Results:A antigenic epitope of human brain Acetylcholinesterase recognized by monoclonal antibody against Torpedo Acetylcholinesterase is received by decapeptide scanning.Conclusion:The antigenic epitope 111 could be recognized by the polycolonal antibody against human brain Acetylcholinesterase and monoclonal antibody against Torpedo Acetylcholinesterase,the results indicate that the epitope is highly conserved in human brain AChE and Torpedo AChE.