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      c-type Lysozymes: what do their introns hide?

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      ScienceOpen Research

      ScienceOpen

      Life sciences, Lysozymes, Introns, Translation, Exons, Enzymes

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          Abstract

          The introns of five c-type lysozymes were translated into amino acid sequences: parts of them corresponded to fragments of biologically active proteins. The amino acid sequences of translated introns seem to have a similar behavior as those arising from exons.

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          Most cited references 10

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          Gapped BLAST and PSI-BLAST: a new generation of protein database search programs

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            Adaptive evolution in the stomach lysozymes of foregut fermenters.

            The convergent evolution of a fermentative foregut in two groups of mammals offers an opportunity to study adaptive evolution at the protein level. The appearance of this mode of digestion has been accompanied by the recruitment of lysozyme as a bacteriolytic enzyme in the stomach both in the ruminants (for example the cow) and later in the colobine monkeys (for example the langur). The stomach lysozymes of these two groups share some physicochemical and catalytic properties that appear to adapt them for functioning in the stomach fluid. To examine the basis for these shared properties, we sequenced langur stomach lysozyme and compared it to other lysozymes of known sequence. Tree analysis suggest that, after foregut fermentation arose in monkeys, the langur lysozyme gained sequence similarity to cow stomach lysozyme and evolved two times faster than the other primate lysozymes. This rapid evolution, coupled with functional and sequence convergence upon cow stomach lysozyme, could imply that positive darwinian selection has driven about 50% of the evolution of langur stomach lysozyme.
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              The human lysozyme gene. Sequence organization and chromosomal localization

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                Author and article information

                Contributors
                (View ORCID Profile)
                Journal
                SOR-LIFE
                ScienceOpen Research
                ScienceOpen
                2199-1006
                08 October 2014
                : 0 (ID: 36f92335-138b-4943-bc61-f1922351138b )
                : 0
                : 1-3
                Affiliations
                [1 ]Molécules de Communication, Museum National d'Histoire Naturelle, 63 rue Buffon, F 75005 Paris, France
                Author notes
                [* ]Corresponding author's e-mail address: pierre.jolles@ 123456wanadoo.fr
                Article
                1928:XE
                10.14293/S2199-1006.1.SOR-LIFE.AJNDRN.v1
                © 2014 Pierre Jollès.

                This work has been published open access under Creative Commons Attribution License CC BY 4.0 , which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. Conditions, terms of use and publishing policy can be found at www.scienceopen.com .

                Page count
                Figures: 1, Tables: 2, References: 10, Pages: 3
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                Original article

                Life sciences

                enzymes, exons, translation, introns, lysozymes

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