PMID: 9434120Jan 20, 1998Paper

A spectroscopic study of glycated bovine alpha-crystallin: investigation of flexibility of the C-terminal extension, chaperone activity and evidence for diglycation

Biochimica Et Biophysica Acta
R BlakytnyM M Sheil

Abstract

The effect of glycating the C-terminal extensions of alpha-crystallin on their flexibility was investigated. In the course of the study the reaction sites were identified and double glycation of single lysine residues was found. Alpha-crystallin was incubated until approximately one mole of the sugar had reacted per subunit of the crystallin. The reaction sites were investigated by mass spectrometry and H NMR spectroscopy, and were found to be principally in the short and flexible C-terminal extensions. The chaperone ability of alpha-crystallin was unaffected by this limited glycation. There was little effect on the flexibility of the C-terminal extensions. This result supports the view that the flexibility of the C-terminal extensions of alpha-crystallin is important for chaperone activity. As alpha-crystallin consists of a mixture of unmodified and phosphorylated subunits, a detailed investigation was undertaken of the reaction of galactose with peptides comprising the C-terminal extensions of alphaA- and alphaB-crystallin. The alphaA peptide was incubated with galactose until 0.79 mole of sugar was bound per mole of peptide and the alphaB peptide reacted until 2.2 moles of galactose had been incorporated. The purified glycat...Continue Reading

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