A novel type of crystallin in the frog eye lens. 35-kDa polypeptide is not homologous to any of the major classes of lens crystallins.
作者： Stanislav I. Tomarev , Rina D. Zinovieva , Svetlana M. Dolgilevich , Sergey V. Luchin , Alexander S. Krayev
DOI: 10.1016/0014-5793(84)80508-6
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摘要: Abstract The nucleotide sequence of a cloned DNA coding for the 35-kDa polypeptide eye lens frog Rana temporaria has been determined. without connectors and poly(A) tract is 889 nucleotides in length shows no homology with sequences other classes crystallins; α-, β-, γ- or δ-crystallins. contains one reading frame 675 length, an apparently intact 3′-non-translated region polyadenylation signal tract; 5′-non- translated lost along part region; this accounts about 1/4 total mRNA length. secondary structure prediction according to Ptitsin-Finkelstein method presence predominantly β-strands only few α-helical regions. We conclude that from belongs new class crystallins which we propose name ϵ-crystallin.
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