MEDLINE Journals

    Amino acid sequence of crayfish (Astacus fluviatilis) trypsin If.

    Authors
    Titani K, Sasagawa T, Woodbury RG, et al. 
    Source
    Biochemistry 1983 Mar 15; 22(6) :1459-65.
    Abstract

    The complete amino acid sequence of trypsin from the crayfish Astacus fluviatilis has been determined. The protein was fragmented with cyanogen bromide after S-carboxymethylation of the reduced disulfide bonds and by trypsin after S-carboxymethylation as well as after succinylation of lysine residues and aminoethylation of the reduced disulfide bonds. Peptides were purified by gel filtration and by reversed-phase high-performance liquid chromatography. Stepwise degradation was performed in a spinning cup sequencer. The enzyme contains 237 amino acid residues and has a molecular weight of 25 030. In contrast to bovine trypsin, it contains three rather than six disulfide bonds which are paired in the same fashion as those in trypsin from Streptomyces griseus. The constituents of the active site of bovine trypsin are present in corresponding positions in the crayfish enzyme. Crayfish trypsin shows 43.6% sequence identity with the bovine enzyme as compared to 40.0% identity with the S. griseus enzyme. The present analysis affords the first detailed view into the evolution of trypsins at the invertebrate level.

    Mesh
    Amino Acid Sequence
    Amino Acids
    Animals
    Astacoidea
    Digestive System
    Hydrolysis
    Species Specificity
    Trypsin
    Language

    eng

    Pub Type(s)
    Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.
    PubMed ID

    6838862

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