Crocodilian τ-crystallin: overexpression, purification, and characterization

Mishra, Anurag Kumar ; Chandrashekhar, Reena ; Aggarwal, Ramesh K. ; Sharma, Yogendra (2002) Crocodilian τ-crystallin: overexpression, purification, and characterization Protein Expression and Purification, 25 (1). pp. 59-64. ISSN 1046-5928

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Official URL: http://www.sciencedirect.com/science/article/pii/S...

Related URL: http://dx.doi.org/10.1006/prep.2001.1609

Abstract

τ-Crystallin is a taxon-restricted crystallin found in eye lenses of reptiles and a few avian species but presumably absent in mammals. The level of τ-crystallin in the lens varies among different species. In the crocodile lens, it is the least abundant crystallin and is present in trace amounts. We present a method for cloning, overexpression, and purification of crocodilian τ-crystallin utilizing a combination of gel filtration and ion-exchange chromatography yielding an extremely purified protein. The protein gets profusely expressed resulting in a fairly high yield and exists as a monomeric entity of 47.5 kDa molecular mass. The recombinant τ-crystallin exists in a properly folded native state as probed by circular dichroism and fluorescence spectroscopy and exhibits enolase activity.

Item Type:Article
Source:Copyright of this article belongs to Elsevier Science.
Keywords:τ-crystallin; Crocodile; α-enolase; Lens
ID Code:50872
Deposited On:27 Jul 2011 13:22
Last Modified:27 Jul 2011 13:22

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