470 Weber St. N., Suite 204, Waterloo, ON, Canada N2L 6J2

Call Us: 1-855-885-8288

BSI BSI
  • Home
  • About Us
    • About Us
    • Careers
    • News
    • Conferences
    • Distributors
  • Products
    • Discovery based
      • What to Select
      • PEAKS Studio
      • PEAKS Online
      • PEAKS CMD
      • PEAKS Q (Add-On)
      • PEAKS IMS (Coming Soon)
    • Antibody based
      • PEAKS AB Software
      • Antibody Sequencing Service
      • Ile/Leu Differentiation Service
    • PEAKS Components
      • de novo Peptide Sequencing
      • Database Searching
      • PTM Analysis
      • Peptide Mutations
      • Multi-Engine Peptide ID
      • PEAKS Q (Add-On)
    • Purchase Info
      • Pricing Request
      • Service Plan Subscription
  • Free Trial
    • Download PEAKS Studio
  • Help & Support
    • Self Help
      • FAQ
      • Video Tutorials
      • User Manuals
      • Supported Data Formats
      • Versions of PEAKS
      • Mass Reference
    • Application Notes
      • Walkthrough Tutorial
      • de novo Introduction
      • Database Search Scoring
      • False Discovery Rate
      • Quantification Algorithms
      • Peptide Feature Area
      • Label-Free Quantification (Coming Soon)
      • SILAC Quantification
    • Community
      • Workshops
      • Online Training
      • Testimonials
      • User Publications
      • BSI Publications
      • User Forum
  • Contact Us

Addressing proteolytic efficiency in enzymatic degradation therapy for celiac disease

0
On August 2, 2016February 7, 2017By BSIIn User Publications

Rey, M., et al. Addressing proteolytic efficiency in enzymatic degradation therapy for celiac disease. Scientific Reports. 30980. 02/08/2016.

Characterization of a heat-resistant extracellular protease from Pseudomonas fluorescens 07A shows that low temperature treatments are more effective in deactivating its proteolytic activityCharacterization of a heat-resistant extracellular protease from Pseudomonas fluorescens 07A shows that low temperature treatments are more effective in deactivating its proteolytic activityAmblyomin-X having a Kunitz-type homologous domain, is a noncompetitive inhibitor of FXaand induces anticoagulation in vitro and in vivo

Share this post?

Tweet

About author

BSI (BSI)

Tweets by @PEAKSProteomics

Socials

  • Facebook
  • LinkedIn
  • Twitter
  • Blogger
  • YouTube

Solutions

  • Products & Services
  • PEAKS Studio
  • PEAKS Online
  • PEAKS CMD
  • PEAKS AB Software

Help

  • Online Training
  • Workshops
  • FAQ
  • User Manuals
  • Contact Us

Contact

  • Bioinformatics Solutions Inc.
  • 470 Weber St. N., Suite 204 Waterloo, ON, Canada N2L 6J2
  • Phone: 1-855-885-8288
  • Office Hours: 9:00am - 5:00pm
  • Privacy Policy
© 2020 | Bioinformatics Solutions Inc.