Purification, crystallization and X-ray characterization of a Kunitz-type trypsin inhibitor protein from the seeds of chickpea (Cicer arietinum)
Title | Purification, crystallization and X-ray characterization of a Kunitz-type trypsin inhibitor protein from the seeds of chickpea (Cicer arietinum) |
Publication Type | Journal Article |
Year of Publication | 2011 |
Authors | Sharma, U, Suresh, CG |
Journal | Acta Crystallographica Section F-Structural Biology and Crystallization Communications |
Volume | 67 |
Pagination | 714-717 |
Date Published | JUN |
ISSN | 1744-3091 |
Abstract | {A Kunitz-type trypsin inhibitor protein (CPTI) purified from chickpea seeds was estimated to have a molecular mass of 18 kDa on SDS-PAGE. The IC50 value of CPTI was determined to be 2.5 mu g against trypsin. The inhibitory activity of CPTI is 114 TIU (trypsin inhibitory units) per milligram of protein, which is high compared with those of other known Kunitz-type trypsin inhibitors from legumes. CPTI crystallized in three different orthorhombic crystal forms: P2(1)2(1)2 form A, P2(1)2(1)2 form B and P2(1)2(1)2(1). The crystals of P2(1)2(1)2 form angstrom, with unit-cell parameters a = 37.2 |
DOI | 10.1107/S1744309111015338 |
Type of Journal (Indian or Foreign) | Foreign |
Impact Factor (IF) | 0.86 |
Divison category:
Biochemical Sciences