Abstract
Crystallina constitute 80–90% of the soluble protein of the ocular lens. There are a surprisingly large number of crystallin gene families; some (α- and ßγ-crystallins) are present in all vertebrate lenses, whereas others (the enzyme-crystallins) are found only in the lenses of certain species. The enzyme-crystallins are not lens-specific and appear to have a double function, i.e., as structural proteins in the lens and as metabolic enzymes in other tissues (see Wistow and Piatigorsky, 1988; Piatigorsky and Wistow, 1989). In addition to their lens-specific or lens-preferred expression, the synthesis of the crystallin polypeptides is developmentally regulated in a temporal and spatial manner in the lens (see McAvoy, 1981; Piatigorsky, 1981).
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Chepelinsky, A.B., Wawrousek, E.F., Dubin, R.A., Jaworski, C.J., McDermott, J.B., Piatigorsky, J. (1991). Transcriptional Control of the α-Crystallin Gene Family. In: Obrecht, G., Stark, L.W. (eds) Presbyopia Research. Perspectives in Vision Research. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-2131-7_1
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DOI: https://doi.org/10.1007/978-1-4757-2131-7_1
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