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. 1983 Feb;71(2):341–349. doi: 10.1104/pp.71.2.341

Amino Acid Sequence of Mung Bean Trypsin Inhibitor and Its Modified Forms Appearing during Germination 1

Karl A Wilson 1,2, Jean C Chen 1
PMCID: PMC1066035  PMID: 16662828

Abstract

The amino acid sequence of the major trypsin inhibitor, F, of ungerminated mung beans (Vigna radiata [L.] Wilczek) was determined by a combination of automatic solid phase and manual sequencing techniques. F is a typical Bowman-Birk-type proteinase inhibitor with 80 amino acid residues and exhibits a high degree of identity with the other sequenced members of the Bowman-Birk family of inhibitors. Thin layer peptide maps of mung bean inhibitors E and C (which appear during germination) indicate that both are derived from inhibitor F by limited specific proteolysis. Loss of the carboxyl-terminal residues 77 to 80 from F produces inhibitor E, while the loss of an additional two carboxyl-terminal residues, the loss of the amino-terminal residues 1 to 8, and an internal cleavage at Ala35-Asp36 produces inhibitor C from E. Another inhibitor species, E′, was isolated from ungerminated seeds. It differs from F in the loss of residues 1 to 6. The majority of the proteolytic cleavages noted in the F-E-C-E′ system are at peptide bonds involving aspartyl residues.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Baumgartner B., Chrispeels M. J. Partial characterization of a protease inhibitor which inhibits the major endopeptidase present in the cotyledons of mung beans. Plant Physiol. 1976 Jul;58(1):1–6. doi: 10.1104/pp.58.1.1. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Baumgartner B., Chrispeels M. J. Purification and characterization of vicilin peptidohydrolase, the major endopeptidase in the cotyledons of mung-bean seedlings. Eur J Biochem. 1977 Jul 15;77(2):223–233. doi: 10.1111/j.1432-1033.1977.tb11661.x. [DOI] [PubMed] [Google Scholar]
  3. Chrispeels M. J., Boulter D. Control of storage protein metabolism in the cotyledons of germinating mung beans: role of endopeptidase. Plant Physiol. 1975 Jun;55(6):1031–1037. doi: 10.1104/pp.55.6.1031. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Chü H. M., Chi C. W. The isolation and crystallization of two trypsin inhibitors of low molecular weight from mung bean (Phaseolus aureus Roxb.). Sci Sin. 1965 Oct;14(10):1441–1453. [PubMed] [Google Scholar]
  5. DAVIS B. J. DISC ELECTROPHORESIS. II. METHOD AND APPLICATION TO HUMAN SERUM PROTEINS. Ann N Y Acad Sci. 1964 Dec 28;121:404–427. doi: 10.1111/j.1749-6632.1964.tb14213.x. [DOI] [PubMed] [Google Scholar]
  6. KOSTKA V., CARPENTER F. H. INHIBITION OF CHYMOTRYPSIN ACTIVITY IN CRYSTALLINE TRYPSIN PREPARATIONS. J Biol Chem. 1964 Jun;239:1799–1803. [PubMed] [Google Scholar]
  7. Kiyohara T., Yokota K., Masaki Y., Matsui O., Iwasaki T., Yoshikawa M. The amino acid sequences of proteinase inhibitors I-A and I-A' from adzuki beans. J Biochem. 1981 Sep;90(3):721–728. doi: 10.1093/oxfordjournals.jbchem.a133526. [DOI] [PubMed] [Google Scholar]
  8. Lai C. Y. Regeneration of amino acids from anilinothiazolinones. Methods Enzymol. 1977;47:369–373. doi: 10.1016/0076-6879(77)47038-1. [DOI] [PubMed] [Google Scholar]
  9. Lorensen E., Prevosto R., Wilson K. A. The Appearance of New Active Forms of Trypsin Inhibitor in Germinating Mung Bean (Vigna radiata) Seeds. Plant Physiol. 1981 Jul;68(1):88–92. doi: 10.1104/pp.68.1.88. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Odani S., Ikenaka T. Studies on soybean trypsin inhibitors, XII. Linear sequences of two soybean double-headed trypsin inhibitors, D-II and E-I. J Biochem. 1978 Mar;83(3):737–745. doi: 10.1093/oxfordjournals.jbchem.a131967. [DOI] [PubMed] [Google Scholar]
  11. Odani S., Ikenaka T. Studies on soybean trypsin inhibitors. IV. Complete amino acid sequence and the anti-proteinase sites of Bowman-Birk soybean proteinase inhibitor. J Biochem. 1972 May;71(5):839–848. doi: 10.1093/oxfordjournals.jbchem.a129833. [DOI] [PubMed] [Google Scholar]
  12. Udenfriend S., Stein S., Böhlen P., Dairman W., Leimgruber W., Weigele M. Fluorescamine: a reagent for assay of amino acids, peptides, proteins, and primary amines in the picomole range. Science. 1972 Nov 24;178(4063):871–872. doi: 10.1126/science.178.4063.871. [DOI] [PubMed] [Google Scholar]
  13. Wachter E., Machleidt W., Hofner H., Otto J. Aminopropyl glass and its p-phenylene diisothiocyanate derivative, a new support in solid-phase Edman degradation of peptides and proteins. FEBS Lett. 1973 Sep 1;35(1):97–102. doi: 10.1016/0014-5793(73)80585-x. [DOI] [PubMed] [Google Scholar]
  14. Waxdal M. J., Konigsberg W. H., Henley W. L., Edelman G. M. The covalent structure of a human gamma G-immunoglobulin. II. Isolation and characterization of the cyanogen bromide fragments. Biochemistry. 1968 May;7(5):1959–1966. doi: 10.1021/bi00845a046. [DOI] [PubMed] [Google Scholar]
  15. Wilson K. A., Laskowski M., Sr The partial amino acid sequence of trypsin inhibitor II from garden bean, Phaseolus vulgaris, with location of the trypsin and elastase-reactive sites. J Biol Chem. 1975 Jun 10;250(11):4261–4267. [PubMed] [Google Scholar]
  16. Zhang Y., Luo S., Tan F., Qi Z., Xu L., Zhang A. Complete amino acid sequence of mung bean trypsin inhibitor. Sci Sin B. 1982 Mar;25(3):268–277. [PubMed] [Google Scholar]

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