Literature DB >> 6191764

Biochemistry and applications of aprotinin, the kallikrein inhibitor from bovine organs.

H Fritz, G Wunderer.   

Abstract

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.

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Year:  1983        PMID: 6191764

Source DB:  PubMed          Journal:  Arzneimittelforschung        ISSN: 0004-4172


  73 in total

1.  Directed evolution of antibody fragments with monovalent femtomolar antigen-binding affinity.

Authors:  E T Boder; K S Midelfort; K D Wittrup
Journal:  Proc Natl Acad Sci U S A       Date:  2000-09-26       Impact factor: 11.205

Review 2.  The hemostatic defect of cardiopulmonary bypass.

Authors:  Matthew Dean Linden
Journal:  J Thromb Thrombolysis       Date:  2003-12       Impact factor: 2.300

3.  Tri-domain bifunctional inhibitor of metallocarboxypeptidases A and serine proteases isolated from marine annelid Sabellastarte magnifica.

Authors:  Maday Alonso-del-Rivero; Sebastian A Trejo; Mey L Reytor; Monica Rodriguez-de-la-Vega; Julieta Delfin; Joaquin Diaz; Yamile González-González; Francesc Canals; Maria Angeles Chavez; Francesc X Aviles
Journal:  J Biol Chem       Date:  2012-03-12       Impact factor: 5.157

4.  Chemical semisynthesis of aprotinin homologues and derivatives mutated in P' positions.

Authors:  C Groeger; H R Wenzel; H Tschesche
Journal:  J Protein Chem       Date:  1991-10

5.  Cleavage of influenza a virus hemagglutinin in human respiratory epithelium is cell associated and sensitive to exogenous antiproteases.

Authors:  Oleg P Zhirnov; Mine R Ikizler; Peter F Wright
Journal:  J Virol       Date:  2002-09       Impact factor: 5.103

6.  The histochemical pattern of mechanically or chemically injured rabbit cornea after aprotinin treatment: relationships with the plasmin concentration of the tear fluid.

Authors:  J Cejková; Z Lojda; S Dropcová; D Kadlecová
Journal:  Histochem J       Date:  1993-06

7.  Proteolytic activity and fatal gram-negative sepsis in burned mice: effect of exogenous proteinase inhibition.

Authors:  A N Neely; R G Miller; I A Holder
Journal:  Infect Immun       Date:  1994-06       Impact factor: 3.441

Review 8.  Aprotinin. A review of its pharmacology and therapeutic efficacy in reducing blood loss associated with cardiac surgery.

Authors:  R Davis; R Whittington
Journal:  Drugs       Date:  1995-06       Impact factor: 9.546

9.  The outer surface protein A of the spirochete Borrelia burgdorferi is a plasmin(ogen) receptor.

Authors:  H Fuchs; R Wallich; M M Simon; M D Kramer
Journal:  Proc Natl Acad Sci U S A       Date:  1994-12-20       Impact factor: 11.205

10.  [Aprotinin and recombinant human erythropoietin reduce the need for homologous blood transfusion in cardiac surgery].

Authors:  M Osaka; I Fukuda; H Ohuchi
Journal:  Jpn J Thorac Cardiovasc Surg       Date:  1998-09
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