Abstract
SUMMARY: From 250 g of carp hepatopancreas, 0.29 mg of the purified enzyme was obtained. The bond specificity of cathepsin S for α-neoendorphin and neurotensin was 6Arg-7Lys and 3Tyr-4Glu, respectively. The cleavage sites for insulin B-chain were estimated to be the bonds at 3Asn-4Gln, 6Leu-7Cys, 12Val-13Glu, 13Glu-14Ala, 16Tyr-17Leu, 22Arg-23Gly, 24Phe-25Phe and 26Tyr-27Thr. P2 position on these peptides were bulky and hydrophobic amino acid residues such as Phe or Leu, small amino acid residues such as Gly, Ala and Val were also accepted in these positions. Regarding the protein substrates, cathepsin S degraded carp α-actinin, actin, tropomyosin and troponins T and I although the proteolyzing speeds were distinct from one another.
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