July 1978
Volume 17, Issue 7
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Articles  |   July 1978
Studies on lens proteins. I. Subunit structure of beta crystallins of rabbit lens cortex.
Investigative Ophthalmology & Visual Science July 1978, Vol.17, 660-666. doi:
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      M K Mostafapour, V N Reddy; Studies on lens proteins. I. Subunit structure of beta crystallins of rabbit lens cortex.. Invest. Ophthalmol. Vis. Sci. 1978;17(7):660-666.

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      © ARVO (1962-2015); The Authors (2016-present)

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Abstract

A method has been developed to isolate and characterize beta-crystallins of rabbit lens cortex. Chromatographic separation of water-soluble structure proteins of rabbit lens cortex on a Sephacryl S-200 gel column yielded four beta-crystallin peaks (beta1, beta2, beta3 and beta4), all eluting between alpha and gamma-crystallins. Their molecular weights were estimated to be 250,000, 130,000, 60,000, and 37,000 daltons, respectively. SDS-gradient gel electrophoresis of these beta-crystallins gave rise to characteristic polypeptides; beta1, two polypeptides of 30,000 and 23,000 daltons; beta2, one major polypeptide of 33,000; beta3; two polypeptides of 28,000 and 26,000; and beta4, two polypeptides of 22,500 and 11,200 daltons. From a knowledge of the molecular weights and the ratio of the polypeptides in each crystallin, their oligomeric structure was calculated to be 5:5, 4, 1:1, and 1:1. The relative abundance of these four beta-crystallins was found to be 25.6%, 7.2%, 27.2%, and 2.8% of the total water-soluble proteins of the lens cortex.

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