Purification, crystallization and preliminary crystallographic studies of a Kunitz-type proteinase inhibitor from tamarind (Tamarindus indica) seeds.
A Kunitz-type proteinase inhibitor has been purified from tamarind (Tamarindus indica) seeds. SDS-PAGE analysis of a purified sample showed a homogeneous band corresponding to a molecular weight of 21 kDa. The protein was identified as a Kunitz-type proteinase inhibitor based on N-terminal amino-acid sequence analysis. It was crystallized by the vapour-diffusion method using PEG 6000. The crystals belonged to the orthorhombic space group C222(1), with unit-cell parameters a = 37.2, b = 77.1, c = 129.1 A. Diffraction data were collected to a resolution of 2.7 A. Preliminary crystallographic analysis indicated the presence of one proteinase inhibitor molecule in the asymmetric unit, with a solvent content of 44%.
Patil
Dipak N
DN
Department of Biotechnology, Indian Institute of Technology, Roorkee 247667, India.
Chaudhry
Anshul
A
Sharma
Ashwani K
AK
Tomar
Shailly
S
Kumar
Pravindra
P
D003460:Crystallization; D018360:Crystallography, X-Ray; D004591:Electrophoresis, Polyacrylamide Gel; D010455:Peptides / Q000737:chemistry* / Q000302:isolation & purification*; D010940:Plant Proteins / Q000737:chemistry* / Q000302:isolation & purification*; D012639:Seeds / Q000737:chemistry*; D029861:Tamarindus / Q000737:chemistry*
C053865:Kunitz-type protease inhibitor, plant; D010455:Peptides; D010940:Plant Proteins