Amino acid sequence and disulfide bridges of affinity purified Kunitz-type chymotrypsin inhibitor from winged bean seed (Psophocarpus tetragonolobus (L.) DC).Biochem Int. 1990 Nov; 22(3):543-51.BI
Abstract
The primary sequence of the affinity purified chymotrypsin inhibitor, WBCI, isolated from the albumin fraction of Psophocarpus tetragonolobus (L.) DC cv. UPS-122 seed was determined. The inhibitor consisted of a single polypeptide chain of 183 amino acids (Mr 20285) and the four half-cystine residues in the molecule formed two intramolecular disulfide bridges equivalent to those in other Kunitz-type seed inhibitors. The sequence of this chymotrypsin inhibitor was identical to that of chymotrypsin inhibitor-3 from cultivar UPS-31 and it showed about 50% sequence similarity to the winged bean acidic (WBTI-2, pI 5.1) and basic (WBTI-1, pI 8.9) trypsin inhibitors. Sequence similarities to other Kunitz-type seed inhibitors are discussed.
MeSH
Pub Type(s)
Journal Article
Language
eng
PubMed ID
2076111
Citation
Kortt, A A., et al. "Amino Acid Sequence and Disulfide Bridges of Affinity Purified Kunitz-type Chymotrypsin Inhibitor From Winged Bean Seed (Psophocarpus Tetragonolobus (L.) DC)." Biochemistry International, vol. 22, no. 3, 1990, pp. 543-51.
Kortt AA, Burns JE, Strike PM. Amino acid sequence and disulfide bridges of affinity purified Kunitz-type chymotrypsin inhibitor from winged bean seed (Psophocarpus tetragonolobus (L.) DC). Biochem Int. 1990;22(3):543-51.
Kortt, A. A., Burns, J. E., & Strike, P. M. (1990). Amino acid sequence and disulfide bridges of affinity purified Kunitz-type chymotrypsin inhibitor from winged bean seed (Psophocarpus tetragonolobus (L.) DC). Biochemistry International, 22(3), 543-51.
Kortt AA, Burns JE, Strike PM. Amino Acid Sequence and Disulfide Bridges of Affinity Purified Kunitz-type Chymotrypsin Inhibitor From Winged Bean Seed (Psophocarpus Tetragonolobus (L.) DC). Biochem Int. 1990;22(3):543-51. PubMed PMID: 2076111.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR
T1 - Amino acid sequence and disulfide bridges of affinity purified Kunitz-type chymotrypsin inhibitor from winged bean seed (Psophocarpus tetragonolobus (L.) DC).
AU - Kortt,A A,
AU - Burns,J E,
AU - Strike,P M,
PY - 1990/11/1/pubmed
PY - 1990/11/1/medline
PY - 1990/11/1/entrez
SP - 543
EP - 51
JF - Biochemistry international
JO - Biochem Int
VL - 22
IS - 3
N2 - The primary sequence of the affinity purified chymotrypsin inhibitor, WBCI, isolated from the albumin fraction of Psophocarpus tetragonolobus (L.) DC cv. UPS-122 seed was determined. The inhibitor consisted of a single polypeptide chain of 183 amino acids (Mr 20285) and the four half-cystine residues in the molecule formed two intramolecular disulfide bridges equivalent to those in other Kunitz-type seed inhibitors. The sequence of this chymotrypsin inhibitor was identical to that of chymotrypsin inhibitor-3 from cultivar UPS-31 and it showed about 50% sequence similarity to the winged bean acidic (WBTI-2, pI 5.1) and basic (WBTI-1, pI 8.9) trypsin inhibitors. Sequence similarities to other Kunitz-type seed inhibitors are discussed.
SN - 0158-5231
UR - https://www.unboundmedicine.com/medline/citation/2076111/Amino_acid_sequence_and_disulfide_bridges_of_affinity_purified_Kunitz_type_chymotrypsin_inhibitor_from_winged_bean_seed__Psophocarpus_tetragonolobus__L___DC__
DB - PRIME
DP - Unbound Medicine
ER -