RESUMO
14-S mRNA from rat lens codes for two subunits of alpha-crystallin, A2 (Mr 20 000) and AIns (Mr 24 000, previously referred to as alphaX). Structural relationship between both translation products has been proved by immunoprecipitation with antisera directed against the different crystallin classes. Competition immunoprecipitation showed that the 14-S mRNA translation products are precipitated by common antibodies, specific for the A subunit of alpha-crystallin. Two-dimensional gel electrophoresis and peptide analysis provided further evidence that the 24 000-Mr polypeptide, synthesized in vitro under direction of 14-S mRNA, is identical with native alphaAIns. Although the structures of alphaA2 and alphaAIns are very similar, no precursor-product relationship exists between both 14-S-mRNA-encoded polypeptides.
Assuntos
Cristalinas/genética , Cristalino/metabolismo , Peptídeos , RNA Mensageiro/metabolismo , Animais , Cristalinas/biossíntese , Peso Molecular , Biossíntese Peptídica , Fragmentos de Peptídeos/análise , Testes de Precipitina , Biossíntese de Proteínas , Coelhos , RatosRESUMO
Messenger RNA has been isolated from rat lens tissue. The mRNA species which codes for the A2 chain of alpha-crystallin, revealed the same extremely high sedimentation value (14S) as the corresponding messenger from calf lens. However, it has been shown that in rat lens the 14-S messenger preparation directs the synthesis of an additional alpha-crystallin chain, designated as alpha-X with an approximate molecular weight of 24000. For comparative purpose crystallin synthesis has also been studied as well in cultured rat lens cells as in the rat lens cell-free system.
