Aprotinin

Aprotinin, also known as pancreatic trypsin inhibitor and trypsin-kallikrein inhibitor, is a monomeric polypeptide of 58 amino acids found in a number of organs, including lungs, spleen, liver, and pancreas. It is also detectable in a free form in calf serum. It is a competitive inhibitor that forms a loose complex with serine proteases and blocks their active centers. The complex exhibits many interactions between protease and inhibitor. The trypsin-aprotinin complex, for example, does not dissociate at a concentration of 8 M uric acid or 6 M guanidine hydrochloride. Aprotinin is only cleaved slowly by most proteases, with the exception of thermolysin at temperatures >+60°C. Its unique structure is responsible for the molecule’s high stability and remarkable resistance to elevated temperatures, acids, and proteases.

L'aprotinine est largement utilisée comme inhibiteur de la trypsine.

L'aprotinine est un inhibiteur compétitif de sérine protéase qui forme des complexes stables avec les sites actifs de l'enzyme et les bloque. Cette fixation est réversible, et la plupart des complexes aprotinine-protéase se dissocient aux pH extrêmes (> 10 ou < 3). En terme de structure, l'aprotinine est une protéine globulaire monomère issue de poumon de bovin, constituée de 58 acides aminés disposés de façon à former une chaîne polypeptidique unique comportant trois réticulations (ponts disulfure).

Features:

1. Qualified Raw Materials: Products that meet the stringent requirements of the Elevated Assurance Program, ensuring compliance with regulatory standards.
2. Comprehensive Documentation: Includes essential documents such as certificates, impurity profiles, and declarations to support audits and risk assessments.
3. M-Clarity^™ Quality Attributes: Products are classified within the MQ300 quality segment or higher, demonstrating superior quality assurance. M-Clarity^™ Program
4. Confirmed Process Controls: Established processes that ensure consistency and reliability in manufacturing.
5. Enhanced Change Notification: Timely updates on any changes to product specifications or processes, ensuring transparency and compliance.
6. Freely Available Dossiers: Access to robust, ready-to-present product dossiers that include:
   1. Site quality assessment
   2. ISO 9001 certificate
   3. Detailed product specifications
   4. Relevant declarations/statements (e.g., animal origin content, BSE/TSE, nitrosamine)

Benefits:

1. Regulatory Compliance: Helps you meet compliance standards effectively, reducing the risk of regulatory issues.
2. Audit Readiness: Instills confidence during audits with comprehensive documentation and confirmed process controls, demonstrating your commitment to high-quality products.
3. Operational Transparency: Supports supply chain transparency, allowing you to track and verify the quality of raw materials.
4. Enhanced Support: Provides exceptional quality-related information and tailored assistance to meet your specific needs.
5. Risk Mitigation: Facilitates thorough risk assessments with detailed documentation, helping you manage potential compliance challenges.
6. Informed Decision-Making: Access to clear and comprehensive product information enables better decision-making and enhances operational efficiency.

Une unité d'inhibiteur de trypsine (TIU) réduit de 50 % l'activité de deux unités de trypsine, une unité de trypsine hydrolysant 1,0 μmole de p-nitroanilide de N-alpha-benzoyl-DL-arginine par minute à pH 7,8 et 25 °C. Une autre unité fréquemment rencontrée est la KIU : 1 TIU = 1 300 KIU.

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