@article { ISI:000291216800020,
	title = {Purification, crystallization and X-ray characterization of a Kunitz-type trypsin inhibitor protein from the seeds of chickpea (Cicer arietinum)},
	journal = {Acta Crystallographica Section F-Structural Biology and Crystallization Communications},
	volume = {67},
	number = {6},
	year = {2011},
	month = {JUN},
	pages = {714-717},
	publisher = {WILEY-BLACKWELL},
	address = {111 RIVER ST, HOBOKEN 07030-5774, NJ USA},
	abstract = {<p>{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</p>},
	issn = {1744-3091},
	doi = {10.1107/S1744309111015338},
	author = {Sharma, Urvashi and Suresh, C. G.}
}
