Natural Proteins
Product List
Aprotinin Protein
Aprotinin
Introduction
Aprotinin, also known as Trasylol, is a small protein derived from bovine lung tissue. It is classified as a serine protease inhibitor and is commonly referred to as bovine pancreatic trypsin inhibitor (BPTI) . Aprotinin is primarily used as an antifibrinolytic agent to reduce bleeding during complex surgeries such as heart and liver surgeries .
Key Biological Properties: Aprotinin is a monomeric globular polypeptide consisting of 58 amino acids. It has a molecular weight of approximately 6,512 Da and contains three disulfide bridges that contribute to its stable tertiary structure .
Expression Patterns and Tissue Distribution: Aprotinin is naturally found in bovine lung tissue and other tissues. It is not endogenously produced in humans but is administered exogenously for therapeutic purposes .
Primary Biological Functions: Aprotinin functions as a broad-spectrum protease inhibitor, targeting enzymes such as trypsin, chymotrypsin, plasmin, and kallikrein . It plays a crucial role in modulating the systemic inflammatory response associated with cardiopulmonary bypass surgery .
Role in Immune Responses and Pathogen Recognition: Aprotinin’s inhibition of proteases helps regulate the inflammatory response, which is essential in immune function and pathogen recognition .
Mechanisms with Other Molecules and Cells: Aprotinin forms stable complexes with serine proteases, blocking their active sites and inhibiting their activity . This inhibition is reversible, with complexes dissociating at extreme pH levels .
Binding Partners and Downstream Signaling Cascades: Aprotinin binds to proteases such as trypsin, chymotrypsin, and plasmin, preventing the activation of the intrinsic pathway of coagulation and fibrinolysis . This action helps reduce blood loss during surgeries .
Regulatory Mechanisms Controlling Expression and Activity: Aprotinin’s activity is regulated by its binding to target proteases. The inhibition of proteases like kallikrein and plasmin is concentration-dependent, with specific inhibitory concentrations required for effective action .
Transcriptional Regulation and Post-Translational Modifications: As aprotinin is not endogenously produced in humans, its regulation is primarily through exogenous administration and dosage control .
Biomedical Research: Aprotinin is used in research to study protease activity and inhibition. It is also employed in the purification of enzymes such as urokinase, trypsin, and chymotrypsin .
Diagnostic Tools: Small amounts of aprotinin can be added to blood samples to stabilize certain proteins for laboratory measurements .
Therapeutic Strategies: Aprotinin is used to reduce perioperative blood loss and the need for blood transfusions in high-risk patients undergoing surgeries like coronary artery bypass graft surgery .
