| Literature DB >> 3548817 |
K Titani, H J Torff, S Hormel, S Kumar, K A Walsh, J Rödl, H Neurath, R Zwilling.
Abstract
The amino acid sequence of a protease from the crayfish Astacus fluviatilis has been determined from overlapping sets of peptides derived largely by cleavage at Met, Lys, or Arg residues. The protein comprises 200 amino acid residues in a single polypeptide chain, corresponding to a molecular mass of 22,614 daltons. Two disulfide bonds link Cys-42 to Cys-198 and Cys-64 to Cys-84. The sequence of this invertebrate protease appears to be unique since it has no homologous relationship to any of the known protein sequences.Entities:
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Year: 1987 PMID: 3548817 DOI: 10.1021/bi00375a029
Source DB: PubMed Journal: Biochemistry ISSN: 0006-2960 Impact factor: 3.162