Sequence and immunological characterisation of ovine pancreatic lipase

Purified ovine pancreatic lipase has been subjected to a limited protein sequence analysis. Cyanogen bromide fragments from the molecule were isolated and characterised to enable the structure of the molecule to be mapped. Some tryptic peptides were also isolated, sequenced, and aligned by homology to lipase sequences from other species. A total of 172 residues out of a possible 456 have been assigned, including 45 residues at the N-terminus and 10 residues at the C-terminus of the protein. A polyclonal antibody has been prepared to ovine lipase which has been characterised by Ouchterlony immunodiffusion and by Western blotting experiments. These experiments showed that the ovine pancreatic lipase was immunologically different from the ovine hepatic and lingual lipase, whereas there was considerable immunological similarity amongst ovine, bovine and rabbit pancreatic lipase, but less with porcine pancreatic lipase.