BOVINE PANCREATIC PREPROELASTASE-I AND PREPROELASTASE-II - COMPARISONOF NUCLEOTIDE AND AMINO-ACID-SEQUENCES AND TISSUE-SPECIFIC EXPRESSION

Clones encoding bovine preproelastases I and II were isolated from a p ancreatic cDNA library and were sequenced in order to define the struc tural characteristics of these enzymes. The bovine 947- and 884-nucleo tide preproelastase I and II cDNAs encode proteins containing a signal peptide of the same length (16 amino acids), but with a slightly diff erent number of amino acids for the activation peptide (10 and 12, res pectively) and the mature enzyme (240 and 241, respectively). Consider ing amino acid sequences, each enzyme shares a high degree of identity (76-86%) within species. In contrast, only 55.3% identity is found be tween bovine elastases I and II. This difference could explain partly their own specificity. Analysis of the expression of the elastases in various bovine tissues demonstrated that they are specifically express ed in high levels in the pancreatic gland. These two approaches (struc ture and expression) allowed us to characterize the bovine pancreatic elastases I and II. (C) 1997 Elsevier Science Inc.