M. Gestin et al., BOVINE PANCREATIC PREPROELASTASE-I AND PREPROELASTASE-II - COMPARISONOF NUCLEOTIDE AND AMINO-ACID-SEQUENCES AND TISSUE-SPECIFIC EXPRESSION, Comparative biochemistry and physiology. B. Comparative biochemistry, 118(1), 1997, pp. 181-187
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.