τ-crystallin from the turtle lens: Purification and partial characterization

Williams, Leah A.; Ding, Linlin; Horwitz, Joseph; Piatigorsky, Joram

doi:10.1016/0014-4835(85)90143-5

Cited by 34 publications

(21 citation statements)

References 25 publications

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“…The CD signature profile. profile is in good agreement with the only published report of the secondary structure of -crystallin from turtle lens and matches closely in appearance (5). This Trp Microenvironment Steady-state protein fluorescence is a powerful tool to probe the folding state of the molecule by assessing the microenvironment of Trp, which also provides an insight into its tertiary structure.…”

Section: Chromatographic Purificationsupporting

confidence: 84%

“…The emission maximum is seen at around 330 nm, which indicates that Trp is buried in the hydrophobic environment. The emission maximum of crocodilian -crystallin is close to that of turtle -crystallin, which is 328 nm (5). Taken together, the farand near-UV CD spectra and the fluorescence spectra strongly suggest that the recombinant protein is properly folded and is in a native conformation (Fig.…”

Section: Chromatographic Purificationmentioning

confidence: 80%

“…-Crystallin dom primers and oligo(dT) primer. was first identified and characterized from lamprey and turtles (4, 5) and thus was named as (tau; derived Primer Design and RT-PCR from turtle) (5). Later, it was also found in duck lens Primers for -crystallin were designed from the seand was shown to have sequence identity to ␣ -enolase quence of -crystallin cDNA (7).…”

Section: Rna Isolation -Crystallin Is An Important Taxon-specific Crymentioning

confidence: 99%

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Crocodilian τ-Crystallin: Overexpression, Purification, and Characterization

Mishra

Chandrashekhar

Aggarwal

et al. 2002

Protein Expression and Purification

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Section: Chromatographic Purificationsupporting

confidence: 84%

Section: Chromatographic Purificationmentioning

confidence: 80%

Section: Rna Isolation -Crystallin Is An Important Taxon-specific Crymentioning

confidence: 99%

See 1 more Smart Citation

Crocodilian τ-Crystallin: Overexpression, Purification, and Characterization

Mishra

Chandrashekhar

Aggarwal

et al. 2002

Protein Expression and Purification

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“…Corneas obtained from different embryonic developmental stages (stages [21][22][23][24][25] and from a two-week old crocodile were sectioned and stained for the presence of s-crystallin. The cornea obtained from embryos of stages earlier than 21st were fragile and were not studied.…”

Section: Expression Of S-crystallin In Crocodile Cornea During Embryomentioning

confidence: 99%

“…We have found that a taxon-specific lens crystallin, s-crystallin ⁄ a-enolase, is expressed in the crocodile corneal epithelium as a corneal crystallin. s-Crystallin was first identified in turtle lens [22] and is also expressed in the lenses of duck [23] and lamprey [5]. We have reported earlier that s-crystallin is present in crocodile lens, though as a minor fraction [24].…”

mentioning

confidence: 99%

Triose phosphate isomerase, a novel enzyme‐crystallin, and τ‐crystallin in crocodile cornea

Kathiresan¹,

Krishnan²,

Krishnakumar

et al. 2006

The FEBS Journal

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Crystallins are defined as lens structural proteins, which are classified as ubiquitous a-, b-and c-crystallins, and taxon-specific crystallins [1]. The transparency and refractive properties of lens depends on crystallins. Taxon-specific crystallins are generally enzymes recruited as structural proteins in the lens to perform specialized functions, i.e., maintaining lens transparency [2]. Some examples of the species-specific crystallins are d-and e-crystallins present in birds and reptiles, s-crystallins in turtle and reptiles, q-crystallins in frog and camel lenses [3]. Several of these crystallins are metabolic enzymes: d-crystallin is argininosuccinate lyase [4]; s-crystallin is a-enolase [5]. They are believed to be recruited by gene sharing or by gene duplication [2,6].Some enzymes such as aldehyde dehydrogenase class 3 (ALDH3), aldehyde dehydrogenase class 1 Several enzymes are known to accumulate in the cornea in unusually high concentrations. Based on the analogy with lens crystallins, these enzymes are called corneal crystallins, which are diverse and species-specific. Examining crystallins in lens and cornea in multiple species provides great insight into their evolution. We report data on major proteins present in the crocodile cornea, an evolutionarily distant taxon. We demonstrate that s-crystallin ⁄ a-enolase and triose phosphate isomerase (TIM) are among the major proteins expressed in the crocodile cornea as resolved by 2D gel electrophoresis and identified by MALDI-TOF. These proteins might be classified as putative corneal crystallins. s-Crystallin, known to be present in turtle and crocodile lens, has earlier been identified in chicken and bovine cornea, whereas TIM has not been identified in the cornea of any species. Immunostaining showed that s-crystallin and TIM are concentrated largely in the corneal epithelium. Using western blot, immunofluorescence and enzymatic activity, we demonstrate that high accumulation of s-crystallin and TIM starts in the late embryonic development (after the 24th stage of embryonic development) with maximum expression in a two-week posthatched animal. The crocodile corneal extract exhibits significant a-enolase and TIM activities, which increases in the corneal extract with development. Our results establishing the presence of s-crystallin in crocodile, in conjunction with similar reports for other species, suggest that it is a widely prevalent corneal crystallin. Identification of TIM in the crocodile cornea reported here adds to the growing list of corneal crystallins.Abbreviations ALDH, aldehyde dehydrogenase; IEF, isoelectric focusing; TIM, triose phosphate isomerase.

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Crystallin distribution patterns in concentric layers from toad eye lenses

et al. 2009

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Protein distribution patterns across eye lenses from the Asiatic toad Bufo gargarizans were investigated and individual crystallin classes characterised. Special fractionation that follows the growth mode of the lens was used to yield nine fractions corresponding to layers laid down at different chronological (developmental) stages. Proportions of soluble and insoluble crystallins within each fraction were measured by Bradford assay. Water-soluble proteins in all fractions were separated by size-exclusion HPLC and constituents of each class further characterised by electrophoresis, RP-HPLC and MS analysis. In outer lens layers, alpha-crystallin is the most abundant soluble protein but is not found in soluble proteins in the lens centre. Water-soluble beta-crystallins also decrease from their highest level in the outer lens to negligible mounts in the central lens. The proportion of soluble gamma-crystallin increases significantly towards the lens centre where this is the only soluble protein present. Insoluble protein levels increase significantly towards the lens centre. In B. gargarizans lenses, as with other anurans, the predominant water-soluble protein class is gamma-crystallin. No taxon-specific crystallins were found. The relationship between the protein distribution patterns and the functional properties of the lens this species is discussed.

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τ-crystallin from the turtle lens: Purification and partial characterization

Cited by 34 publications

References 25 publications

Crocodilian τ-Crystallin: Overexpression, Purification, and Characterization

Crocodilian τ-Crystallin: Overexpression, Purification, and Characterization

Triose phosphate isomerase, a novel enzyme‐crystallin, and τ‐crystallin in crocodile cornea

Crystallin distribution patterns in concentric layers from toad eye lenses

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