Biochemistry and applications of aprotinin, the kallikrein inhibitor from bovine organs.
نویسندگان
چکیده
The basic proteinase inhibitor from bovine organs, aprotinin (active ingredient of Trasylol) has been extensively studied with respect to its chemical, physical and biochemical properties and its inhibitory mechanism of action. It is widely used as a valuable tool for studying protein/protein interactions and protein conformation at the molecular level. There are numerous examples of the usefulness of aprotinin in biochemical and biomedical research. It has also become a valuable drug for the treatment of various diseases like, e.g. hyperfibrinolytic hemorrhage and traumatic-hemorrhagic shock. The purpose of this paper is threefold. It summarizes our present knowledge of the subject in various disciplines; it provides the active scientist with basic data for his experimental work; and above all it points the way to future directions of aprotinin research.
منابع مشابه
Kinetics of inhibition of human plasma kallikrein by a site-specific modified inhibitor Arg15-aprotinin: evaluation using a microplate system and comparison with other proteases.
Human plasma kallikrein, a product of contact-activated plasma proteolysis, is moderately inhibited by aprotinin, a small polypeptide from bovine lung that has been used as an experimental drug in human disease states. Aprotinin has a Lys residue in the P1 (reactive center) position occupying residue 15. Since kallikrein is an arginine-directed serine protease, we hypothesized that an altered f...
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Human plasma kallikrein. a product of contact-activated plasma proteolysis. is moderately inhibited by aprotinin. a small polypeptide from bovine lung that has been used as an experimental drug in human disease states. Aprotinin has a Lys residue in the P1 (reactive center) position occupying residue 1 5. Since kallikrein is an argininedirected serine protease. we hypothesized that an altered f...
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ورودعنوان ژورنال:
- Arzneimittel-Forschung
دوره 33 4 شماره
صفحات -
تاریخ انتشار 1983