Occurrence of two distinct molecular species of cathepsin B in carp Cyprinus carpio |
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| Authors: | Yan Tan Kiyoshi Osatomi Yukinori Nozaki Tadashi Ishihara Kenji Hara |
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| Institution: | Graduate School of Science and Technology, Nagasaki University, Bunkyo and;Faculty of Fisheries, Nagasaki University, 1-14 Bunkyo-machi, Nagasaki 852-8521, Japan |
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| Abstract: | ABSTRACT: 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, we cloned carp cathepsin B cDNA. The nucleotide sequence of carp cathepsin B cDNA consists of 1470 bp including a 993 bp open reading frame, encoding a deduced protein of 330 amino acids. The deduced amino acid sequence of carp cathepsin B has similarity of 80% to rainbow trout cathepsin B and of 76–78% to other vertebrate cathepsins B. The sequence of its isoform was also determined during molecular cloning, which has 94.8% similarity with first cloned cathepsin B. They are completely same in N-terminal amino acid sequence of heavy chain, active site and potential N-glycosylation site. This indicates there are at least two kinds of cathepsin B functioning in vivo in carp. |
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| Keywords: | carp cathepsin B isoform lysosomal cysteine proteinase molecular cloning purification |
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