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- W1966293411 abstract "We have investigated the origins of the two major size classes of delta-crystallin polypeptides (48 kDa and 50 kDa on sodium dodecyl sulfate-urea-polyacrylamide gels) in the chicken lens. Both the 48-kDa and 50-kDa polypeptides were produced by cell-free translation in a salt-dependent (Na+, K+, acetate and Cl-) pattern from mRNA derived from a cloned delta 1-crystallin cDNA. The salt-dependent alteration in the ratio of cell-free synthesis of the 48-kDa to 50-kDa delta-crystallin polypeptides was greatly enhanced by capping of the delta 1 mRNA. Translation of the delta 1 mRNA containing a premature termination codon suggested that the larger delta-crystallin band contains two polypeptides which differ in their N-terminal one-third. In vitro transcription/translation analysis of several mutant delta 1 cDNA clones and immunoblot analysis of authentic delta-crystallin with antisera raised to peptides contained in delta-crystallin showed that neither alternative initiation at two in-phase AUG codons nor alternative termination at sites on the delta 1 mRNA are responsible for generating the two sizes of the delta-crystallin polypeptides. Taken together our data suggest (but do not prove) that delta-crystallin heterogeneity is generated by co-translational modification of the primary polypeptide encoded in the delta 1-crystallin gene." @default.
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- W1966293411 date "1987-01-01" @default.
- W1966293411 modified "2023-09-23" @default.
- W1966293411 title "Expression of the δ1-crystallin gene: salt-dependent alteration in the cell-free synthesis of δ-crystallin polypeptides" @default.
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- W1966293411 doi "https://doi.org/10.1016/0378-1119(87)90372-6" @default.
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