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| Content Provider | Springer Nature Link |
|---|---|
| Author | Atta, Ambreen Ilyas, Amber Hashim, Zehra Ahmed, Aftab Zarina, Shamshad |
| Copyright Year | 2014 |
| Abstract | Taxon specific lens crystallins in vertebrates are either similar or identical with various metabolic enzymes. These bifunctional crystallins serve as structural protein in lens along with their catalytic role. In the present study, we have partially purified and characterized lens crystallin from Indian spiny-tailed lizard (Uromastyx hardwickii). We have found lactate dehydrogenase (LDH) activity in lens indicating presence of an enzyme crystallin with dual functions. Taxon specific lens crystallins are product of gene sharing or gene duplication phenomenon where a pre-existing enzyme is recruited as lens crystallin in addition to structural role. In lens, same gene adopts refractive role in lens without modification or loss of pre-existing function during gene sharing phenomenon. Apart from conventional role of structural protein, LDH activity containing crystallin in U. hardwickii lens is likely to have adaptive characteristics to offer protection against toxic effects of oxidative stress and ultraviolet light, hence justifying its recruitment. Taxon specific crystallins may serve as good models to understand structure–function relationship of these proteins. |
| Starting Page | 128 |
| Ending Page | 134 |
| Page Count | 7 |
| File Format | |
| ISSN | 15723887 |
| Journal | The Protein Journal |
| Volume Number | 33 |
| Issue Number | 2 |
| e-ISSN | 15734943 |
| Language | English |
| Publisher | Springer US |
| Publisher Date | 2014-02-06 |
| Publisher Place | New York |
| Access Restriction | One Nation One Subscription (ONOS) |
| Subject Keyword | ε-Crystallin Gene recruitment Gene sharing Lactate dehydrogenase Reptilian lens Taxon specific crystallin Bioorganic Chemistry Biochemistry Organic Chemistry Animal Anatomy / Morphology / Histology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Organic Chemistry Analytical Chemistry Biochemistry Bioengineering |
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