The Primary Structure of Porcine Glandular Kallikreins

Publisher Website
Google Scholar
Abstract
The amino acid sequence of the A- and B-chains of porcine pancreatic kallikrein B is presented and compared to that of porcine trypsin. The overall homology between both enzymes is 37% identical residues in corresponding position and 51% chemically similar resideus. Comparison of the sequences with the crystal structure of bovine trypsin reveals that the trypsin "autolysis loop" is enlarged in kallikrein by two residues but lacks the basic residue at the cleavage site. Substitutions at the calcium-binding site of trypsin which include Arg 70 for Glu 70 possibly interfere with ion binding. Insertions between trypsin residues 95 and 96 obviously form a new kallikrein "autolysis loop" containing the site of cleavage between the A- and B-chains. One carbohydrate moiety is attached to this surface loop at Asn 95, the second to Asn 239 at the same edge of the globular molecule. The residues at the surface of the substrate binding site are substituted to an extent of 85% while the residues forming contacts to the trypsin inhibitor (Kunitz) are highly preserved. Immunodiffusion studies as well as identity of the N-terminal sequences of pancreatic, submandibular and urinary kallikrein reveal the same genetic origin of the three glandular kallikreins.