Abstract:
:The current study reports several post-translational modifications of alphaB-crystallin in normal human lenses. The isoforms of post-translational modified alphaB-crystallin were isolated from the normal human lenses of >70-age group by ion exchange chromatography and sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The isoform modifications were determined in detail by fast atom bombardment mass spectroscopy and amino acid sequence analysis. As the criterion of non-modified alphaB-crystallin, alphaB-crystallin from 1-d-old infant lenses were used. The modifications found in this study involve oxidation of the N-terminal methionine-1 residue, phosphorylation of the serine-59 residue, and truncation of four amino acids from the C-terminal position of the crystallin. The oxidation of methionine-1 was found in the early stage of human life in 1-d-old lens, although other modification of alphaB-crystallin were usually only found in old lenses (>70-age group).
journal_name
Biol Pharm Bulljournal_title
Biological & pharmaceutical bulletinauthors
Kamei A,Hamaguchi T,Matsuura N,Iwase H,Masuda Kdoi
10.1248/bpb.23.226subject
Has Abstractpub_date
2000-02-01 00:00:00pages
226-30issue
2eissn
0918-6158issn
1347-5215journal_volume
23pub_type
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