Argall ME.Amino acid sequence of a trypsin/chymotrypsin inhibitor from giant taro(Alocasia macrorrhiza). BBA Protein Struct Mol Enzymol . 1994Argall, M.E., Bradbury, J.H., and Shaw, D.C. (1994). Amino-acid sequence of a trypsin/chymotrypsin inhibitor from giant taro (Alocasia macror...
Nichino J , Takano R , Kamei-Hayashi K , Minakata H , Nomoto K , Hara S ( 1992 ): Amino acid sequences of trypsin inhibitors from oriental pickling melon( Cucumis melo L. var. Conomon Makino) seeds . Biosci Biotech Biochem 56 : 1241 – 1246 ....
(MATOUv1 + metaT)30,31and PhyloDB databases32, using the BLASTP-algorithm based identification combined with hmmsearch analysis. The BLASTP-algorithm based search was conducted using trypsin amino acid sequences from NCBI and UniProt database as queries with an e-value ≤1e−5 as the...
As a potential alternative candidate, Streptomyces griseus trypsin (SGT), which is composed of 223 resi- dues with a molecular weight of 23.1 kDa, has 34.2% homology with bovine trypsin in amino acid sequence, including the active site residues (H57, D102 and S195), substrate binding ...
Trypsin cleaves only those peptide bonds in which the carboxyl group is contributed by a lysine or an arginine residue, regardless of the length or amino acid sequence of the chain. Our Immobilized TPCK Trypsin can be substituted for free trypsin in many application and is advantageous because ...
[60]. Other microbial proteases are more distantly related, having shorter amino acid sequences and corresponding surface loops. For instance, α-lytic protease has the same fold as trypsin, but differs greatly in many structural aspects[61]. Many other serine proteases such as the kallikreins,...
Purifica- tion, amino acid sequence, and cDNA cloning of trypsin in- hibitors from onion (Allium cepa L.) bulbs. Biosci Biotechnol Biochem 2003;67:1653-1659.M. Deshimaru, A. Watanabe, K. Suematsu, M. Hatano, S. Terada, Purification, amino acid sequence, and cDNA cloning of trypsin ...
Keywords: Amino acid sequence; atypical binding sites; Bowman−Birk inhibitor; chymotrypsin inhibitor; disulfide bridges; Glycine max; inhibition of bovine proteinases; inhibition of human proteinases; Lens culinaris; lentil; lima bean; Phaseolus lunatus; primary structure; reactive sites; soybean; ...
The amino acid sequence of barley trypsin inhibitor has been determined. The protein is a single polypeptide consisting of 121 amino acid residues and has Mr = 13,305. No free sulfhydryl groups were detected by Ellman's reagent, which indicates the presence of five disulfide bridges in the mol...
The complete amino acid sequence was determined by automatic degradation, and by DABITC/PITC microsequence analysis of peptides obtained from enzyme digestions of the reduced and S-carboxymethylated protein with trypsin, chymotrypsin, elastase, the Glu-specific protease from S. aureus and the Lys-...