PMID: 6479167Sep 17, 1984

Primary structure of Vicia angustifolia proteinase inhibitor

European Journal of Biochemistry
Y ShimokawaO Abe

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.

References

Sep 1, 1975·Analytical Biochemistry·E Mendez, C Y Lai
Mar 1, 1979·FEBS Letters·C IshikawaK Takahashi
Jun 1, 1978·Journal of Biochemistry·O AbeK Kuromizu
Feb 1, 1977·Analytical Biochemistry·C L ZimmermanJ J Pisano
Nov 21, 1972·Biochemistry·M A HermodsonK A Walsh
Feb 1, 1974·Archives of Biochemistry and Biophysics·R J Knights, A Light
Feb 21, 1967·Biochimica Et Biophysica Acta·K R Woods, K T Wang
Sep 1, 1981·Journal of Biochemistry·T KiyoharaM Yoshikawa
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Jan 1, 1946·The Journal of General Physiology·M KUNITZ

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