Study on separation and analysis of anticoagulant compounds for anticoagulant activity in vitro on mixture of peptide from pepsin enzymolysis of centipede.
- Author:
Li JIANG
1
;
Yurong WANG
;
Shaohua ZHAO
;
Nengting HUANG
Author Information
- Publication Type:Journal Article
- MeSH: Animals; Anticoagulants; isolation & purification; metabolism; Arthropods; chemistry; enzymology; Chromatography, High Pressure Liquid; Male; Partial Thromboplastin Time; Pepsin A; chemistry; metabolism; Peptides; isolation & purification; metabolism; Rabbits; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
- From: China Journal of Chinese Materia Medica 2012;37(3):298-301
- CountryChina
- Language:Chinese
-
Abstract:
OBJECTIVETo separate anticoagulant components from the pepsin enzymolysis of centipede by gel filtration and reverse-phase C18 chromatography, and to detect the distribution range of their molecular mass.
METHODCingula and 280 nm ultraviolet spectrometry were used to detect and collect the chromatographic solutions. The components' anticoagulant activity in vitro was detected with activated partial thromboplastin time (APTT) as the index, and the molecular mass range of the active composition was detected by MALDI-TOF-MS.
RESULTAnticoagulant active compounds were produced by gel filtration and reverse-phase C18 chromatography. The distribution range of relative molecular mass was determined to be from 597 to 1 146.
CONCLUSIONGel filtration and reverse-phase C18 chromatography are feasible for separating and purifying the pepsin enzymolysis of Centipede. The anticoagulant active compounds are oligopeptides.
