Identification of cDNAs encoding two novel rat pancreatic serine proteases.
Serine proteases (SPs) are a family of physiologically important and versatile enzymes. We designed degenerated oligodeoxyribonucleotide primers derived from the consensus amino acid aa sequences of the active site of mammalian SPs, to selectively amplify in a polymerase chain reaction (PCR) cDNA fragments coding for SPs. We used poly(A)+ RNA from rat pancreas to obtain the cDNA. Two of the amplified cDNA fragments encode novel SPs. The full-length nucleotide sequence of both cDNAs was also obtained by PCR. The high degree of homology to trypsins and elastases suggests that the cDNAs encode a trypsin-like and an elastase-like SP, respectively. Both mRNAs were also found to occur, to a lesser extent, in spleen, as was the case for the mRNAs of other rat pancreatic SPs.
Kang
J
J
Institut für Genetik, Universität zu Köln, F.R.G.
Wiegand
U
U
Müller-Hill
B
B
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D015152:Blotting, Northern; D003001:Cloning, Molecular; D015870:Gene Expression; D008969:Molecular Sequence Data; D010179:Pancreas / Q000201:enzymology*; D010196:Pancreatic Elastase / Q000737:chemistry / Q000235:genetics*; D016133:Polymerase Chain Reaction; D051381:Rats; D012689:Sequence Homology, Nucleic Acid; D014357:Trypsin / Q000737:chemistry / Q000235:genetics*
D010196:Pancreatic Elastase; D014357:Trypsin