Abstract:
:In the present study a thiol proteinase inhibitor was isolated from buffalo kidney making use of ammonium sulphate precipitation and gel filtration chromatography on Sephacryl S-100HR column. Purified inhibitor is homogeneous as it displayed a single band in gel electrophoresis both under reducing and non-reducing environment and is of 65KDa as revealed by gel filtration and SDS PAGE. Kinetic studies revealed the presence of reversible accompanied with competitive mode of inhibition; showing maximum efficacy against papain (Ki=2.90×10-4). It was maximally active at pH 8.0 and was stable for a period of 30, 60 and 90 days at 37, 4 and -20°C respectively. Immunological studies confirmed its purity of epitopes as a single precipitin line is obtained in immunodiffusion. N-terminal analysis revealed that it shared a good homology with mouse kidney cystatin as well as with Human Cys C and Cys E thereby advocating its use as a model for various human oriented studies which targets how the kidney cystatin level varies in accordance with various drugs that are currently being used as a target for variety of diseases.
journal_name
Int J Biol Macromoljournal_title
International journal of biological macromoleculesauthors
Shamsi A,Ahmed A,Bano Bdoi
10.1016/j.ijbiomac.2015.12.084subject
Has Abstractpub_date
2017-01-01 00:00:00pages
819-826issue
Pt Beissn
0141-8130issn
1879-0003pii
S0141-8130(15)30271-3journal_volume
94pub_type
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journal_title:International journal of biological macromolecules
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journal_title:International journal of biological macromolecules
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abstract::This article has been withdrawn at the request of the author(s) and/or editor. The Publisher apologizes for any inconvenience this may cause. The full Elsevier Policy on Article Withdrawal can be found at https://www.elsevier.com/about/our-business/policies/article-withdrawal. ...
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