A low molecular weight peptide from Allium porum with inhibitory activity on platelet aggregation in vitro.
A peptide factor was isolated from Allium porum with strong inhibitory activity on platelet aggregation induced by collagen or ADP. The peptide was isolated by a series of chromatographic techniques and purified to homogeneity by HPLC on RP C8 column. Its molecular weight, as it was estimated by plasma desorption mass spectrometry, is 1052 Da. Amino acid analysis showed the presence of Phe, Asp, Ser, Thr, Arg and Pro.
Liakopoulou-Kyriakides
M
M
Dept. of Chemical Engineering, Aristotle University of Thessaloniki, Greece.
Sinakos
Z
Z
D000490:Allium / Q000737:chemistry*; D002851:Chromatography, High Pressure Liquid; D013058:Mass Spectrometry; D010940:Plant Proteins / Q000302:isolation & purification / Q000494:pharmacology*; D010975:Platelet Aggregation Inhibitors / Q000302:isolation & purification / Q000494:pharmacology*
D010940:Plant Proteins; D010975:Platelet Aggregation Inhibitors