Literature DB >> 8883101

Molecular masses of gamma-crystallins.

M L Riley1, J J Harding, G W Kilby, R J Truscott, A Aquilina, M M Sheil.   

Abstract

Bovine gamma-crystallins were isolated and analysed by electrospray mass spectrometry (ESMS). The mass of gamma II-crystallin was as predicted from the amino acid sequence and the mass of gamma IIIb-crystallin was close, but the mass of gamma IVa-crystallin was 59 Da greater than that expected. gamma IVa-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 gamma IVa-crystallin, which has been used to predict its three-dimensional structure, is incorrect.

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Year:  1996        PMID: 8883101     DOI: 10.1159/000267968

Source DB:  PubMed          Journal:  Ophthalmic Res        ISSN: 0030-3747            Impact factor:   2.892


  2 in total

1.  Malformation of junctional microdomains in cataract lens membranes from a type II diabetes patient.

Authors:  Stéphanie Mangenot; Nikolay Buzhynskyy; Jean-François Girmens; Simon Scheuring
Journal:  Pflugers Arch       Date:  2008-11-26       Impact factor: 3.657

2.  Gamma III-crystallin is the primary target of glycation in the bovine lens incubated under physiological conditions.

Authors:  Hong Yan; Antony C Willis; John J Harding
Journal:  Biochem J       Date:  2003-09-15       Impact factor: 3.857

  2 in total

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