Crossref journal-article
Wiley
European Journal of Biochemistry (311)
Abstract

The main polypeptide chain of the lens protein α‐crystallin (αA2) is N‐terminally acetylated and contains two methionine residues. The chain is initiated by the incorporation of a methionine residue exclusively donated by methionyl‐tRNArMet.This N‐terminal methionine is not removed during polypeptide chain synthesis. The internal methionine residue is donated exclusively by one of the methionyl‐tRNAMet species. When lens messenger RNA coding for the αrA2 chain is translated in a reticulocyte cell‐free system, the newly synthesized polypeptide chain carries an acetylated methionine in the N‐terminal position.

Bibliography

Strous, G. J. A. M., Berns, T. J. M., van Westernen, H., & Bloemendal, H. (1972). Synthesis of Lens Protein in vitro Role of Methionyl‐tRNAs in the Synthesis of Calf‐Lens α‐Crystallin. European Journal of Biochemistry, 30(1), 48–52. Portico.

Dates
Type When
Created 20 years, 5 months ago (March 3, 2005, 9:57 a.m.)
Deposited 1 year, 9 months ago (Nov. 22, 2023, 4:47 p.m.)
Indexed 1 year, 9 months ago (Nov. 23, 2023, 11:19 a.m.)
Issued 52 years, 10 months ago (Oct. 1, 1972)
Published 52 years, 10 months ago (Oct. 1, 1972)
Published Online 20 years, 5 months ago (March 3, 2005)
Published Print 52 years, 10 months ago (Oct. 1, 1972)
Funders 0

None

@article{Strous_1972, title={Synthesis of Lens Protein in vitro Role of Methionyl‐tRNAs in the Synthesis of Calf‐Lens α‐Crystallin}, volume={30}, ISSN={1432-1033}, url={http://dx.doi.org/10.1111/j.1432-1033.1972.tb02070.x}, DOI={10.1111/j.1432-1033.1972.tb02070.x}, number={1}, journal={European Journal of Biochemistry}, publisher={Wiley}, author={Strous, Ger J. A. M. and Berns, Ton J. M. and van Westernen, Hanske and Bloemendal, Hans}, year={1972}, month=oct, pages={48–52} }