Identification of cDNAs encoding two novel rat pancreatic serine proteases |
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Authors: | Jie Kang Ulrich Wiegand Benno Müller-Hill |
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Institution: | Institut für Genetik der Universität zu Köln, D-5000, Cologne 41, F.R.G. |
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Abstract: | 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-lenght 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. |
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Keywords: | Trypsin elastase PCR amplification degenerated primer design expression pattern sequence homology recombinant DNA |
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