Ruminant Stomach

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Taiji Imoto - One of the best experts on this subject based on the ideXlab platform.

  • colonic lysozymes of rabbit japanese white recent divergence and functional conversion
    Journal of Biochemistry, 1994
    Co-Authors: Yuji Ito, Masaki Hirashima, Hidenori Yamada, Taiji Imoto
    Abstract:

    Lysozyme was extracted from the feces of rabbit (Japanese White) with 2.5% acetic acid and purified by ion-exchange chromatography. Subsequent ion-exchange HPLC at pH 4.0 revealed the presence of two isozymes, namely rabbit colonic lysozymes 1 and 2. The amino acid sequences of these lysozymes were determined. The colonic lysozymes 1 and 2 showed 98% identity with each other and 94 and 95% identities with rabbit kidney lysozyme, respectively. The very high identities between kidney and colonic lysozymes indicate that the colonic isozymes diverged from the conventional kidney lysozyme very recently, probably after the divergence of rabbit from other rodents, accompanying the gene duplication. Despite the small changes in the sequences, the enzymatic properties of colonic lysozyme differ from those of the kidney lysozyme. The activity of the colonic lysozyme against Micrococcus luteus cells showed a narrow and acidic pH optimum, in contrast to the wide and high pH optimum of the kidney lysozyme. Changes in the enzymatic properties are analogous to those of the Ruminant Stomach lysozymes and may implicate adaptive evolution in the functional conversion of rabbit colonic lysozymes in gut.

Yuji Ito - One of the best experts on this subject based on the ideXlab platform.

  • colonic lysozymes of rabbit japanese white recent divergence and functional conversion
    Journal of Biochemistry, 1994
    Co-Authors: Yuji Ito, Masaki Hirashima, Hidenori Yamada, Taiji Imoto
    Abstract:

    Lysozyme was extracted from the feces of rabbit (Japanese White) with 2.5% acetic acid and purified by ion-exchange chromatography. Subsequent ion-exchange HPLC at pH 4.0 revealed the presence of two isozymes, namely rabbit colonic lysozymes 1 and 2. The amino acid sequences of these lysozymes were determined. The colonic lysozymes 1 and 2 showed 98% identity with each other and 94 and 95% identities with rabbit kidney lysozyme, respectively. The very high identities between kidney and colonic lysozymes indicate that the colonic isozymes diverged from the conventional kidney lysozyme very recently, probably after the divergence of rabbit from other rodents, accompanying the gene duplication. Despite the small changes in the sequences, the enzymatic properties of colonic lysozyme differ from those of the kidney lysozyme. The activity of the colonic lysozyme against Micrococcus luteus cells showed a narrow and acidic pH optimum, in contrast to the wide and high pH optimum of the kidney lysozyme. Changes in the enzymatic properties are analogous to those of the Ruminant Stomach lysozymes and may implicate adaptive evolution in the functional conversion of rabbit colonic lysozymes in gut.

David M Irwin - One of the best experts on this subject based on the ideXlab platform.

  • Genomic organization and evolution of Ruminant lysozyme c genes
    Science Press PR China, 2015
    Co-Authors: David M Irwin
    Abstract:

    Ruminant Stomach lysozyme is a long established model of adaptive gene evolution. Evolution of Stomach lysozyme function required changes in the site of expression of the lysozyme c gene and changes in the enzymatic properties of the enzyme. In Ruminant mammals, these changes were associated with a change in the size of the lysozyme c gene family. The recent release of near complete genome sequences from several Ruminant species allows a more complete examination of the evolution and diversification of the lysozyme c gene family. Here we characterize the size of the lysozyme c gene family in extant Ruminants and demonstrate that their pecoran Ruminant ancestor had a family of at least 10 lysozyme c genes, which included at least two pseudogenes. Evolutionary analysis of the Ruminant lysozyme c gene sequences demonstrate that each of the four exons of the lysozyme c gene has a unique evolutionary history, indicating that they participated independently in concerted evolution. These analyses also show that episodic changes in the evolutionary constraints on the protein sequences occurred, with lysozyme c genes expressed in the abomasum of the Stomach of extant Ruminant species showing the greatest levels of selective constraints

Hidenori Yamada - One of the best experts on this subject based on the ideXlab platform.

  • colonic lysozymes of rabbit japanese white recent divergence and functional conversion
    Journal of Biochemistry, 1994
    Co-Authors: Yuji Ito, Masaki Hirashima, Hidenori Yamada, Taiji Imoto
    Abstract:

    Lysozyme was extracted from the feces of rabbit (Japanese White) with 2.5% acetic acid and purified by ion-exchange chromatography. Subsequent ion-exchange HPLC at pH 4.0 revealed the presence of two isozymes, namely rabbit colonic lysozymes 1 and 2. The amino acid sequences of these lysozymes were determined. The colonic lysozymes 1 and 2 showed 98% identity with each other and 94 and 95% identities with rabbit kidney lysozyme, respectively. The very high identities between kidney and colonic lysozymes indicate that the colonic isozymes diverged from the conventional kidney lysozyme very recently, probably after the divergence of rabbit from other rodents, accompanying the gene duplication. Despite the small changes in the sequences, the enzymatic properties of colonic lysozyme differ from those of the kidney lysozyme. The activity of the colonic lysozyme against Micrococcus luteus cells showed a narrow and acidic pH optimum, in contrast to the wide and high pH optimum of the kidney lysozyme. Changes in the enzymatic properties are analogous to those of the Ruminant Stomach lysozymes and may implicate adaptive evolution in the functional conversion of rabbit colonic lysozymes in gut.

Masaki Hirashima - One of the best experts on this subject based on the ideXlab platform.

  • colonic lysozymes of rabbit japanese white recent divergence and functional conversion
    Journal of Biochemistry, 1994
    Co-Authors: Yuji Ito, Masaki Hirashima, Hidenori Yamada, Taiji Imoto
    Abstract:

    Lysozyme was extracted from the feces of rabbit (Japanese White) with 2.5% acetic acid and purified by ion-exchange chromatography. Subsequent ion-exchange HPLC at pH 4.0 revealed the presence of two isozymes, namely rabbit colonic lysozymes 1 and 2. The amino acid sequences of these lysozymes were determined. The colonic lysozymes 1 and 2 showed 98% identity with each other and 94 and 95% identities with rabbit kidney lysozyme, respectively. The very high identities between kidney and colonic lysozymes indicate that the colonic isozymes diverged from the conventional kidney lysozyme very recently, probably after the divergence of rabbit from other rodents, accompanying the gene duplication. Despite the small changes in the sequences, the enzymatic properties of colonic lysozyme differ from those of the kidney lysozyme. The activity of the colonic lysozyme against Micrococcus luteus cells showed a narrow and acidic pH optimum, in contrast to the wide and high pH optimum of the kidney lysozyme. Changes in the enzymatic properties are analogous to those of the Ruminant Stomach lysozymes and may implicate adaptive evolution in the functional conversion of rabbit colonic lysozymes in gut.