tailieunhanh - Báo cáo khoa học: Bovine tryptases cDNA cloning, tissue specific expression and characterization of the lung isoform

A complementary DNA encoding a new bovine tryptase isoform (here named BLT) was cloned and sequenced from lung tissue. Analysis of sequence indicates the pres-ence of a 26-amino acid prepro-sequence and a 245 amino acid catalytic domain. It contains six different residues when compared with the previously characterized tryptase from bovine liver capsule (BLCT), with the most signifi-cant difference residing at the primary specificity S1 pocket. | Eur. J. Biochem. 270 507-517 2003 FEBS 2003 doi Bovine tryptases cDNA cloning tissue specific expression and characterization of the lung isoform Alessandra Gambacurta1 Laura Fiorucci1 Paolo Basili1. Fulvio Erba1. Anaela Amoresano2 B B wW M M BM M w 4 w B 4 fB fB FB B w w B B fB FF B FF BB B B B B B B B w B FF B w BB B BB B BB BB B fB B BB B B FB B BB B fB B B fb and Franca Ascoli1 1Department of Experimental Medicine and Biochemical Sciences University of Rome Tor Vergata Rome department of Organic Chemistry and Biochemistry University of Naples Federico II Naples Italy A complementary DNA encoding a new bovine tryptase isoform here named BLT was cloned and sequenced from lung tissue. Analysis of sequence indicates the presence of a 26-amino acid prepro-sequence and a 245 amino acid catalytic domain. It contains six different residues when compared with the previously characterized tryptase from bovine liver capsule BLCT with the most significant difference residing at the primary specificity S1 pocket. In BLT the canonical residues Asp-Ser are present at positions 188-189 while in BLCT these positions are occupied by residues Asn-Phe. This finding was confirmed by mass fingerprinting of the peptide mixture obtained upon in-gel tryptic digestion of BLT. Analysis by gel filtration of the purified protein shows that BLT is probably tetrameric similar to the previously identified tryptases from other species with monomer migrating as 35-40 kDa multiple bands in SDS PAGE. As expected the catalytic abilities of the two bovine tryptases are different. The specificity constant values kcat Kn assayed with model substrates are 10- to 60-fold higher in the case of BLT. The tissue-specific expression of the two tryptases was evaluated at the RNA level by analysis of their different restriction patterns. In lung only BLT was found to be expressed while in liver capsule only BLCT is present. Both isoforms are distributed in similar amounts in .

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