BIOMAT Database Logo BIOMAT Database Logo

Multiple intermediates in the reaction of bovine beta-trypsin with bovine pancreatic trypsin inhibitor (Kunitz). 1983

E Antonini, and P Ascenzi, and E Menegatti, and M Guarneri

UI MeSH Term Description Entries
D007611 Aprotinin A single-chain polypeptide derived from bovine tissues consisting of 58 amino-acid residues. It is an inhibitor of proteolytic enzymes including CHYMOTRYPSIN; KALLIKREIN; PLASMIN; and TRYPSIN. It is used in the treatment of HEMORRHAGE associated with raised plasma concentrations of plasmin. It is also used to reduce blood loss and transfusion requirements in patients at high risk of major blood loss during and following open heart surgery with EXTRACORPOREAL CIRCULATION. (Reynolds JEF(Ed): Martindale: The Extra Pharmacopoeia (electronic version). Micromedex, Inc, Englewood, CO, 1995) BPTI, Basic Pancreatic Trypsin Inhibitor,Basic Pancreatic Trypsin Inhibitor,Bovine Kunitz Pancreatic Trypsin Inhibitor,Kallikrein-Trypsin Inactivator,Kunitz Pancreatic Trypsin Inhibitor,Trypsin Inhibitor, Basic, Pancreatic,Trypsin Inhibitor, Kunitz, Pancreatic,Antilysin,Bovine Pancreatic Trypsin Inhibitor,Contrical,Contrykal,Dilmintal,Iniprol,Kontrikal,Kontrykal,Pulmin,Traskolan,Trasylol,Zymofren,Inactivator, Kallikrein-Trypsin,Kallikrein Trypsin Inactivator
D007700 Kinetics The rate dynamics in chemical or physical systems.
D011370 Proflavine Topical antiseptic used mainly in wound dressings. 3,6-Diamino Acridine,3,6-Diaminoacridine,Proflavin,Proflavine Hemisulfate,3,6 Diamino Acridine,3,6 Diaminoacridine,Acridine, 3,6-Diamino,Hemisulfate, Proflavine
D011485 Protein Binding The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments. Plasma Protein Binding Capacity,Binding, Protein
D002417 Cattle Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor. Beef Cow,Bos grunniens,Bos indicus,Bos indicus Cattle,Bos taurus,Cow,Cow, Domestic,Dairy Cow,Holstein Cow,Indicine Cattle,Taurine Cattle,Taurus Cattle,Yak,Zebu,Beef Cows,Bos indicus Cattles,Cattle, Bos indicus,Cattle, Indicine,Cattle, Taurine,Cattle, Taurus,Cattles, Bos indicus,Cattles, Indicine,Cattles, Taurine,Cattles, Taurus,Cow, Beef,Cow, Dairy,Cow, Holstein,Cows,Dairy Cows,Domestic Cow,Domestic Cows,Indicine Cattles,Taurine Cattles,Taurus Cattles,Yaks,Zebus
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D014357 Trypsin A serine endopeptidase that is formed from TRYPSINOGEN in the pancreas. It is converted into its active form by ENTEROPEPTIDASE in the small intestine. It catalyzes hydrolysis of the carboxyl group of either arginine or lysine. EC 3.4.21.4. Tripcellim,Trypure,beta-Trypsin,beta Trypsin

Related Publications

E Antonini, and P Ascenzi, and E Menegatti, and M Guarneri
On the reaction of acetamidomethanol with native and reduced bovine pancreatic trypsin inhibtor (Kunitz inhibitor).
January 1976, International journal of peptide and protein research,
E Antonini, and P Ascenzi, and E Menegatti, and M Guarneri
The bovine basic pancreatic trypsin inhibitor (Kunitz inhibitor): a milestone protein.
June 2003, Current protein & peptide science,
E Antonini, and P Ascenzi, and E Menegatti, and M Guarneri
Hydrogen exchange kinetics of bovine pancreatic trypsin inhibitor beta-sheet protons in trypsin-bovine pancreatic trypsin inhibitor, trypsinogen-bovine pancreatic trypsin inhibitor, and trypsinogen-isoleucylvaline-bovine pancreatic trypsin inhibitor.
June 1987, Biochemistry,
E Antonini, and P Ascenzi, and E Menegatti, and M Guarneri
Kinetics of the interaction of bovine pancreatic trypsin inhibitor (Kunitz) with alpha-chymotrypsin.
June 1974, Biochemistry,
E Antonini, and P Ascenzi, and E Menegatti, and M Guarneri
Pancreatic trypsin inhibitor (Kunitz). II. Complexes with proteinases.
January 1972, Cold Spring Harbor symposia on quantitative biology,
E Antonini, and P Ascenzi, and E Menegatti, and M Guarneri
Binding of the bovine basic pancreatic trypsin inhibitor (Kunitz) to human Lys77-plasmin.
September 1986, Journal of molecular biology,
E Antonini, and P Ascenzi, and E Menegatti, and M Guarneri
Refolding of bovine pancreatic trypsin inhibitor via non-native disulphide intermediates.
June 1995, Journal of molecular biology,
E Antonini, and P Ascenzi, and E Menegatti, and M Guarneri
Binding of the bovine basic pancreatic trypsin inhibitor (Kunitz inhibitor) to human and bovine factor Xa. A thermodynamic study.
May 1990, Biological chemistry Hoppe-Seyler,
E Antonini, and P Ascenzi, and E Menegatti, and M Guarneri
Pancreatic trypsin inhibitor. II. Reaction with trypsin.
May 1953, The Biochemical journal,
E Antonini, and P Ascenzi, and E Menegatti, and M Guarneri
Pancreatic trypsin inhibitor (Kunitz). I. Structure and function.
January 1972, Cold Spring Harbor symposia on quantitative biology,
Copied contents to your clipboard!