Abstract:
:A new cleavage site, which is a post-translational modification, was found between residues His-154 and Ala-155 in alpha A-crystallin from the aged human lens. After trypsin digestion of alpha A-crystallin two peptides that include Asp-151 were obtained and have remarkable differences. That is, the stereo-configuration of the Asp-151 in the normal length peptide was predominately inverted to the D-isomer of beta-aspartyl form (D/L of 5.7). However, the stereoconfiguration of the Asp-151 in the cleavage peptide, that lacks the sequence following Ala-155 to the C-terminus, remained predominately in the L-isomer form as indicated by a D/L value of 0.3. The results suggest that the secondary structure in the region of Ala-155 to the C-terminus may constitute a field that causes the inversion of the Asp-151 to the D-isomer form. Since this kind of cleavage was not found in alpha A-crystallin from young lens, the cleavage between His-154 and Ala-155 is probably the result of aging.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Fujii N,Momose Y,Yamasaki M,Yamagaki T,Nakanishi H,Uemura T,Takita M,Ishii Ndoi
10.1006/bbrc.1997.7365subject
Has Abstractpub_date
1997-10-29 00:00:00pages
918-23issue
3eissn
0006-291Xissn
1090-2104pii
S0006-291X(97)97365-4journal_volume
239pub_type
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