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      Molecular Masses of Gamma-Crystallins

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          Abstract

          Bovine γ-crystallins were isolated and analysed by electrospray mass spectrometry (ESMS). The mass of γll-crystallin was as predicted from the amino acid sequence and the mass of γlIIb-crystallin was close, but the mass of γlVa-crystallin was 59 Da greater than that expected. γlVa-Crystallin was digested with cyanogen bromide and the fragments were isolated before analysis by ESMS. The masses of the fragments did not correspond to the published sequence. The published sequence of γlVa-crystallin, which has been used to predict its three-dimensional structure, is incorrect.

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          Author and article information

          Journal
          ORE
          Ophthalmic Res
          10.1159/issn.0030-3747
          Ophthalmic Research
          S. Karger AG
          978-3-8055-6379-6
          978-3-318-01658-1
          0030-3747
          1423-0259
          1996
          1996
          11 December 2009
          : 28
          : Suppl 2
          : 131-135
          Affiliations
          aNuffield Laboratory of Ophthalmology, University of Oxford, UK; bAustralian Cataract Research Foundation, Department of Chemistry, University of Wollongong, Australia
          Article
          267968 Ophthalmic Res 1996;28:131–135
          10.1159/000267968
          8883101
          © 1996 S. Karger AG, Basel

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          Pages: 5
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