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Primary structure of <em>Vicia angustifolia</em> proteinase inhibitor.
- Source :
- European Journal of Biochemistry; 9/17/84, Vol. 143 Issue 3, p677-684, 8p
- Publication Year :
- 1984
-
Abstract
- The complete amino acid sequence (72 amino acid residues) of a double-headed proteinase inhibitor from seeds of Vicia angustifolia L. var. segetalis Koch has been determined and compared with those of other double-headed inhibitors of known structure. Sequencing was performed by conventional methods with the aid of the fragments produced by reduction and S-carboxymethylation of the enzymatically modified inhibitors, and also using tryptic and chymotryptic peptides. The positions of the 14 half-cystine residues agreed among all the reported primary structures of the legume double-headed inhibitors. However, V. angustifolia inhibitor possessed extensive amino acid differences compared to the others. The phylogenetic relationship among these inhibitors was established using the unweighted pair-group method and revealed that the V. angustifolia inhibitor and the peanut inhibitor B-III had diverged at a relatively earlier stage compared to the other inhibitors. [ABSTRACT FROM AUTHOR]
- Subjects :
- AMINO acids
ORGANIC acids
AMINO acid sequence
PROTEOLYTIC enzymes
PEPTIDES
PROTEINS
Subjects
Details
- Language :
- English
- ISSN :
- 00142956
- Volume :
- 143
- Issue :
- 3
- Database :
- Complementary Index
- Journal :
- European Journal of Biochemistry
- Publication Type :
- Academic Journal
- Accession number :
- 15832431
- Full Text :
- https://doi.org/10.1111/j.1432-1033.1984.tb08421.x