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Crystallization and preliminary x-ray diffraction studies on a typsin\chymotrypsin double headed inhibitor from Horsegram.

Prakash, B. and Murthy, M. R. N. and Sreerama, Y. N. and Ramasarma, P. R. and Rajagopal Rao, D. (1994) Crystallization and preliminary x-ray diffraction studies on a typsin\chymotrypsin double headed inhibitor from Horsegram. Journal of Molecular Biology, 235. pp. 364-366.

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Abstract

The Bowman-Birk family of proteinase inhibitors from seeds of leguminous plants usually have a molecular mass of 8000 to 10,000 Da. Horse gram (Dolichos bifloros or Macrotyloma uniflorum) seeds contain an unusual Bowman-Birk inhibitor of molecular mass 15,500 Da active against both trypsin and chymotrypsin. In order to elucidate its three-dimensional structure, its evolutionary relationship with the more usual Bowman-Birk inhibitors and to study the structure-function properties, this inhibitor has been purified and crystallized. The purified protein crystallizes easily under a variety of conditions in different crystal forms. Crystals obtained by precipitating the protein (3 to 5 mg/ml in 50raM Tris'HCI (pH 8"0)) with 5% ammonium sulphate and 2 to 3% PEG 4000 appear to be suitable for structure determination by X-ray diffraction. The crystals belong to cubic space group P213 (a= ll0"81 A) and diffract X-rays to beyond 3"0 A resolution.

Item Type: Article
Uncontrolled Keywords: crystallization; Bowman-Birk; inhibitor; proteinase; horse gram
Subjects: 500 Natural Sciences and Mathematics > 07 Life Sciences > 03 Biochemistry & Molecular Biology
600 Technology > 08 Food technology > 22 Legumes-Pulses
Divisions: Dept. of Biochemistry
Depositing User: Food Sci. & Technol. Information Services
Date Deposited: 15 Jun 2011 05:11
Last Modified: 28 Dec 2011 09:45
URI: http://ir.cftri.com/id/eprint/3648

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