|Title:||Trypsin Inhibitor from the Seeds of Acacia Confusa||Authors:||WU, HAN-CHUNG||Issue Date:||1991||Journal Volume:||v.110||Journal Issue:||n.6||Start page/Pages:||879-83||Source:||JOURNAL OF BIOCHEMISTRY||Abstract:||
A trypsin inhibitor (ACTI) was isolated and purified from the seeds of Acacia confusa by gel filtration, and trypsin- Sepharose 4B column affinity chromatography. The molecular weight of ACTI was found to be 21, 000 +/- 1,000 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and amino acid composition analysis. ACTI contained four half-cystine and no methionine residues, and was rich in aspartic acid, glutamic acid, glycine, leucine, and lysine residues. The native trypsin inhibitor was composed of two polypeptide chains, and it inhibited trypsin and alpha- chymotrypsin stoichiometrically at the molar ratio of 1:1 and 2:1, respectively. The amino-terminal sequence analysis of the A. confusa trypsin inhibitor A and B chains revealed a more extensive homology with Acacia elata and silk tree trypsin inhibitors, and a less extensive homology with Kunitz soybean trypsin inhibitor. respectively. The amino- terminal sequence analysis of the A.
|Appears in Collections:||口腔生物科學研究所|
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.