Product List

Aprotinin Protein

Aprotinin

Aprotinin is a natural proteinase inhibitor polypeptide consisting of fifty-eight amino acids {C284H432N84O79S7} arranged in a single polypeptide chain, cross-linked by three disulfide bridges and having a molecular mass of 6512.
Shipped with Ice Packs
Cat. No.
BT29100
Source
Bovine Lung.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

Introduction

Definition and Classification

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 .

Biological Properties

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 .

Biological Functions

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 .

Modes of Action

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

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 .

Applications

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 .

Role in the Life Cycle

Role Throughout the Life Cycle: Aprotinin’s primary role is during surgical procedures to manage bleeding and reduce the need for blood transfusions. Its use is critical in patients with high bleeding risks, contributing to better surgical outcomes and recovery .

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