doi: 10.1111/j.1432-1033.1977.tb11775.x.
Synthesis of lens protein in vitro: formation of beta-crystallin
- PMID: 913413
- DOI: 10.1111/j.1432-1033.1977.tb11775.x
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Synthesis of lens protein in vitro: formation of beta-crystallin
Eur J Biochem.
1977 Sep.
Free article
Abstract
Upon addition of lens polyribosomes to a reticulocyte-cell-free system, alpha, beta L-, and gamma crystallin are synthesized, while beta H crystallin is not formed. This phenomenon is comparable to the biosynthetic events in the lens-cell-free system and in tissue culture. It is shown that beta H crystallin formation depends upon the presence of a polypeptide beta B1 b which arises by posttranslational modification. The putative precursor for beta B1 b is a polypeptide beta BU a of which the messenger with a sedimentation coefficient of 12.5 S has been isolated.
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