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

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JMB-01-94
 
Title Crystallization and preliminary x-ray diffraction studies on a typsin\chymotrypsin double headed inhibitor from Horsegram.
 
Creator Prakash, B.
Murthy, M. R. N.
Sreerama, Y. N.
Ramasarma, P. R.
Rajagopal Rao, D.
 
Subject 03 Biochemistry & Molecular Biology
22 Legumes-Pulses
 
Description 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.
 
Date 1994
 
Type Article
PeerReviewed
 
Format application/pdf
 
Language en
 
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Identifier http://ir.cftri.com/3648/1/Journal_of_Molecular_Biology%2C_Volume_235%2C_Issue_1%2C_7_January_1994%2C_Pages_364-366.pdf
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.