Cathepsin L-Like Protease from Xenopus Embryos That Is Stimulated by Nucleoside Phosphates and Nucleic Acids

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概要

• 論文の詳細を見る

• An acid thiol protease that was activated at an early stage of embryogenesis was purified from Xenopus embryos. The N-terminal amino acid sequence(16 residues) of the heavy chain of the enzyme was similar to that of cathepsin L. The proteolytic activity of the protease was enhanced by ATP. Other nucleoside triphosphates, AMP and nucleic acids also enhanced the proteolytic activity. The possible mechanism and biological significance of the activation of the protease in Xenopus embryos are discussed.

• 社団法人日本動物学会の論文
• 1995-12-15

著者

• Miyata Shohei

  Department of Chemistry, College of Humanities and Sciences, Nihon University

• Miyata Shohei

  Department Of Chemistry College Of Humanities And Sciences Nihon University

• Kihara H

  Laboratory Of Research For Biosynthesis And Metabolism Keio University School Of Medicine

• Kihara Hirozi

  Laboratory Of Research For Biosynthesis And Metabolism Keio University School Of Medicine

• Kihara K.

  Laboratory of Research for Biosynthesis and Metabolism, Keio University, School of Medicine

関連論文

• Changes in Timing and Site of Appearance of a Protease in Xenopus Embryos(Developmental Biology)
• Hormonal Reversal and the Genetic Control of Sex Differentiation in Xenopus(Biochemistry)
• Inhibition of gastrulation in Xenopus embryos by an antibody against a cathepsin L-like protease
• Cathepsin L-Like Protease from Xenopus Embryos That Is Stimulated by Nucleoside Phosphates and Nucleic Acids
• In Vivo and in Vitro Effects of a Protease Inhibitor (E-64) on Cell Division of Xenopus eggs : Biochemistry
• Analysis of inhibition of topoisomerase IIα and cancer cell proliferation by ingenolEZ

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