Primary structure of kunitz-type trypsin inhibitor-2a (pI 5.9) fromPsophocarpus tetragonolobus (L.) DC seed
- 1 April 1991
- journal article
- research article
- Published by Springer Nature in Protein Journal
- Vol. 10 (2) , 183-188
- https://doi.org/10.1007/bf01024782
Abstract
The primary structure of acidic trypsin inhibitor-2a (WBTI-2a,pI 5.9) fromPsophocarpus tetragonolobus (L.) DC seed was determined. This inhibitor consists of a single polypeptide chain of 180 amino acids including four half-cystine residues and has an N-terminal residue of pyroglutamic acid. The sequence of WBTI-2a,pI 5.9, showed 84% identity to acidic trypsin inhibitor-2 (WBTI-2,pI 5.1) but only 57% identity to the basic trypsin inhibitor (WBTI-1,pI 8.9) and 50% identity to the chymotrypsin inhibitor of winged bean. The data indicate that winged bean seed contains a family of three Kunitz-type inhibitors which have about 50% identity.Keywords
This publication has 17 references indexed in Scilit:
- Amino acid sequence of the acidic kunitz-type trypsin inhibitor from winged-bean seed [Psophocarpus tetragonolobus (L.) DC]Protein Journal, 1990
- Amino acid sequence of a crystalline seed albumin (winged bean albumin‐1) from Psophocarpus tetragonolobus (L.) DCEuropean Journal of Biochemistry, 1989
- Facile analysis and purification of deblocked N-terminal pyroglutamyl peptides with a strong cation-exchange sulfoethyl aspartamide columnBiochemical and Biophysical Research Communications, 1988
- Amino acid sequence of hemoglobin I from root nodules of the non‐leguminous Casuarina glauca‐Frankia symbiosisFEBS Letters, 1988
- The amino acid sequence and reactive (inhibitory) site of the major trypsin isoinhibitor (DE5) isolated from seeds of the Brazilian Carolina tree (Adenanthera pavonina L.)Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1986
- The complete amino-acid sequence of the endogenous α-amylase inhibitor in wheatBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1986
- N-terminal amino acid sequence of trypsin inhibitor 3 from winged beanPhytochemistry, 1983
- Amino acid sequence of pilin from Bacteroides nodosus (strain 198), the causative organism of ovine footrotFEBS Letters, 1983
- Isolation and properties of a chymotrypsin inhibitor from winged bean seed (Psophocarpus tetragonolobus(L) Dc.)Biochimica et Biophysica Acta (BBA) - Protein Structure, 1980
- [14] Cleavage at AsnGly bonds with hydroxylaminePublished by Elsevier ,1977