Purification and Characterization of Trypsin Inhibitor from the Cicer arietinum L. (Chickpea) Sprouts - Abstract
The proteins fraction of chickpea sprout were extracted and purified by two steps of ion-exchange chromatography and high-pressure liquid chromatography (HPLC) for the first time, the peptides components and molecular weights were determined as11079.57 11440.95, 16619.09, 26016.41, 26032.49, 26016.34 and 28822.02 Da by liquid chromatography and mass spectrometer (LC/MS). The major protein component of this 26032.49 kDa fraction was isolated with trypsin inhibitor activity by HPLC and the partial amino acid sequence was determined as the:
(K)LIEAMVEVEGQLCMDVPSNPGTSAPPFAIVHSSGISLPDRQSATPCSAD-DWRPYLV(-).