Protease Inhibitors

Aprotinin from bovine lung is a globular polypeptide monomer with a molecular weight of 6.5 kDa.

Aprotinin from bovine lung is a globular polypeptide monomer with a molecular weight of 6.5 kDa.

Aprotinin is a 58 amino acid-long protein, with a calculated molecular weight of 6512 Da, that acts as a serine protease inhibitor. Known also as bovine pancreatic trypsin inhibitor (BPTI), aprotinin inhibits serine proteases such as chymotrypsin,

Aprotinin is a 58 amino acid-long protein, with a calculated molecular weight of 6512 Da, that acts as a serine protease inhibitor. Known also as bovine pancreatic trypsin inhibitor (BPTI), aprotinin inhibits serine proteases such as chymotrypsin,

Aprotinin is a 58 amino acid-long protein, with a calculated molecular weight of 6512 Da, that acts as a serine protease inhibitor. Known also as bovine pancreatic trypsin inhibitor (BPTI), aprotinin inhibits serine proteases such as chymotrypsin,

Aprotinin is a 58 amino acid-long protein, with a calculated molecular weight of 6512 Da, that acts as a serine protease inhibitor. Known also as bovine pancreatic trypsin inhibitor (BPTI), aprotinin inhibits serine proteases such as chymotrypsin,

Aprotinin is a single chain polypeptide (58 amino-acids) crosslinked by three disulfide bridges, showing competitive and reversible inhibiton of proteolytic and esterolytic activity. Aprotinin forms stable complexes and blocks the active sites of

Aprotinin is a single chain polypeptide (58 amino-acids) crosslinked by three disulfide bridges, showing competitive and reversible inhibiton of proteolytic and esterolytic activity. Aprotinin forms stable complexes and blocks the active sites of

Aprotinin is a single chain polypeptide (58 amino-acids) crosslinked by three disulfide bridges, showing competitive and reversible inhibiton of proteolytic and esterolytic activity. Aprotinin forms stable complexes and blocks the active sites of

Aprotinin is a single chain polypeptide (58 amino-acids) crosslinked by three disulfide bridges, showing competitive and reversible inhibiton of proteolytic and esterolytic activity. Aprotinin forms stable complexes and blocks the active sites of

Aprotinin is a single chain polypeptide (58 amino-acids) crosslinked by three disulfide bridges, showing competitive and reversible inhibiton of proteolytic and esterolytic activity. Aprotinin forms stable complexes and blocks the active sites of

Aprotinin is a single chain polypeptide (58 amino-acids) crosslinked by three disulfide bridges, showing competitive and reversible inhibiton of proteolytic and esterolytic activity. Aprotinin forms stable complexes and blocks the active sites of