Substrate specificity of cathepsin H in untransformed tissues of mammary gland and in tissues of moderately differentiated form of lobular infiltrating breast cancer

The substrate specifity of cathepsin H in untransformed tissues of mammary gland and in tissues of moderately differentiated form of lobular infiltrating breast cancer has been investigated. Cathepsin H from untransformed tissues of mammary gland hydrolyzed synthetic substrates in a row: Bz-Gly-Phe-...

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Bibliographic Details
Main Author: G. Labunets
Format: Article
Language:English
Published: Taras Shevchenko National University of Kyiv 2016-07-01
Series:Vìsnik: Kiïvsʹkij Nacìonalʹnij Unìversitet Imenì Tarasa Ševčenka. Bìologìâ
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Online Access:http://biovestnik.com/index.php/biology/article/view/54
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Summary:The substrate specifity of cathepsin H in untransformed tissues of mammary gland and in tissues of moderately differentiated form of lobular infiltrating breast cancer has been investigated. Cathepsin H from untransformed tissues of mammary gland hydrolyzed synthetic substrates in a row: Bz-Gly-Phe--->Z-Phe-Ala--->Z-Glu- Tyr--->oxytocin unlike enzyme from malignant tumor that did not hydrolyze the synthetic dipeptide Z-Glu-Tyr and revealed the substrate specificity in a row: Z-Phe-Ala--->Bz-Gly-Phe--->oxytocin. Cathepsin H has proteolytic endopeptidase activity to the substrate casein more pronounced for enzyme from untransformed tissue of mammary gland.
ISSN:1728-2748
2308-8036