Sequence analysis of the βB2-crystallin cDNA of hamster containing a domain conserved among vertebrates
The cDNA sequence of the βB2-cry was determined from hamster (Mesocricetus auratus) and compared to the corresponding genes of bovine, frog, chicken, human, mouse and rat. Multispecies comparison demonstrated high homology between the hamster, rat and mouse gene, but larger distances to man, bovine,...
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Veröffentlicht in: | Gene 1996-09, Vol.174 (1), p.181-184 |
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creator | Zarbalis, Konstantinos Chatterjee, Bimal Löster, Jana Werner, Thomas Graw, Jochen |
description | The cDNA sequence of the
βB2-cry was determined from hamster
(Mesocricetus auratus) and compared to the corresponding genes of bovine, frog, chicken, human, mouse and rat. Multispecies comparison demonstrated high homology between the hamster, rat and mouse gene, but larger distances to man, bovine, chicken and frog. There is striking identity within a strech of 36 deduced amino acids (aa) between the Greek key motif 3 and part of motif 4. This 36-aa domain contains a putative phosphorylation site for protein kinase C and is highly conserved among all known basic βB-Cry; however, it can neither be detected in the acidic βAnor in the γ-Cry. |
doi_str_mv | 10.1016/0378-1119(96)00256-9 |
format | Article |
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βB2-cry was determined from hamster
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βB2-cry was determined from hamster
(Mesocricetus auratus) and compared to the corresponding genes of bovine, frog, chicken, human, mouse and rat. Multispecies comparison demonstrated high homology between the hamster, rat and mouse gene, but larger distances to man, bovine, chicken and frog. There is striking identity within a strech of 36 deduced amino acids (aa) between the Greek key motif 3 and part of motif 4. 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βB2-cry was determined from hamster
(Mesocricetus auratus) and compared to the corresponding genes of bovine, frog, chicken, human, mouse and rat. Multispecies comparison demonstrated high homology between the hamster, rat and mouse gene, but larger distances to man, bovine, chicken and frog. There is striking identity within a strech of 36 deduced amino acids (aa) between the Greek key motif 3 and part of motif 4. This 36-aa domain contains a putative phosphorylation site for protein kinase C and is highly conserved among all known basic βB-Cry; however, it can neither be detected in the acidic βAnor in the γ-Cry.</abstract><cop>Netherlands</cop><pub>Elsevier B.V</pub><pmid>8863746</pmid><doi>10.1016/0378-1119(96)00256-9</doi><tpages>4</tpages></addata></record> |
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source | MEDLINE; ScienceDirect Journals (5 years ago - present) |
subjects | Amino Acid Sequence Animals Base Sequence Cattle Conserved Sequence Cricetinae Crystallins - genetics DNA sequence analysis DNA, Complementary - genetics Evolution Eye protein Humans Mesocricetus auratus Mice Molecular Sequence Data Polymerase chain reaction Rats Sequence Alignment Sequence Analysis, DNA |
title | Sequence analysis of the βB2-crystallin cDNA of hamster containing a domain conserved among vertebrates |
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