These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: The complete amino acid sequence of a Kunitz family trypsin inhibitor from seeds of Acacia confusa.
    Author: Wu HC, Lin JY.
    Journal: J Biochem; 1993 Feb; 113(2):258-63. PubMed ID: 8468333.
    Abstract:
    The complete amino acid sequence of a Kunitz-type two-chain trypsin inhibitor was determined for the first time. The sequence of the inhibitor from Acacia confusa (ACTI) was determined by analysis of peptides obtained from the reduced and S-carboxymethylated protein by digestion with endopeptidase Lys-C, endopeptidase Arg-C, and V8 endopeptidase. ACTI is comprised of two chains, namely A and B chains linked by the disulfide bridge between Cys(133) and Cys(141), and the inhibitor consists of 175 amino acid residues, 136 residues in the A-chain and 39 residues in the B-chain. The N-terminal amino acid sequence of ACTI shows extensive homology to the trypsin inhibitors from Acacia elata and Albizzia julibrissin, while the whole amino acid sequence of ACTI has a high degree of homology to the other Kunitz-type trypsin inhibitors from soybeans, winged bean seeds [Psophocarpus tetragonolobus (L) DC.], and seeds of Erythrina species.
    [Abstract] [Full Text] [Related] [New Search]