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We purified cathepsins B1 and B2 from the ordinary muscle of carp Cyprinus carpio. The N-terminal amino acid sequences (12 residues) of 29 kDa bands of cathepsins B1 and B2 are the same and showed high homology of 75% and 83%, respectively, with the heavy chain of rat and human cathepsins B. Based on conserved sequences of other cathepsins B and the N-terminal amino acid sequences of 29 kDa bands,...
The 2474 nucleotides of carp cathepsin B gene (corresponding to the part of open reading frame and 3′non-coding region of cDNA) have been determined by polymerase chain reaction cloning, which was organized into nine exons and eight introns. The boundary sequences of the exon-intron junctions conformed to the GT/AG consensus rule. One polyadenylation signal sequence of AATAAA was found in the 3′non-coding...
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