1. Trypsin

2. Intro  Trypsin is a serine protease found in the digestive system of many vertebrates, where it hydrolyses proteins.  Trypsin is produced in the pancreas.  In 1876, trypsin was first named by Kuhne who described the proteolytic activity of this pancreatic enzyme.

3. Function Trypsin in the duodenum catalyses the hydrolysis of peptide bonds so that proteins can be broken down into smaller peptides. These peptides may then be further hydrolysed into amino acids by other proteases before they enter the blood stream. Tryptic digest is a necessary step in protein absorption because proteins are generally too big to be absorbed through the lining of the small intestine.

4. Diseases One consequence of the autosomal recessive disease cystic fibrosis is a deficiency in transport of trypsin and other digestive enzymes from the pancreas. This leads to the disorder termed meconium ileus. This disorder involves intestinal obstruction (ileus) due to overly thick meconium, which is normally broken down by trypsins and other proteases, then passed in faeces.

5. Structure of trypsin  First gance structure of trypsin First gance structure of trypsin

6. Four Levels of Structure  Primary structure is just a sequence of amino acids.  Secondary Structure includes the shape taken up by parts of amino acid chain.  Tertiary Structure is a three dimensional structure of a protein.  Several polypeptides (individual molecules) may combine to form a larger protein. These polypeptides may be the same or different. The combination of polypeptides in a given protein is called quaternary structure.