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Amino acid sequence of a unique protease from the crayfish Astacus fluviatilis.
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.
PMID: 3548817 [PubMed - indexed for MEDLINE]
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Cited by 10 PubMed Central articles
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Gene cooption without duplication during the evolution of a male-pregnancy gene in pipefish.
Harlin-Cognato A, Hoffman EA, Jones AG.
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[Proc Natl Acad Sci U S A. 2006]
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cDNA cloning, bacterial expression, in vitro renaturation and affinity purification of the zinc endopeptidase astacin.
Reyda S, Jacob E, Zwilling R, Stöcker W.
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[Biochem J. 1999]
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Mueller CG, Rissoan MC, Salinas B, Ait-Yahia S, Ravel O, Bridon JM, Briere F, Lebecque S, Liu YJ.
J Exp Med. 1997 Aug 29; 186(5):655-63.
[J Exp Med. 1997]
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