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. 1991 Aug;96(4):1086–1092. doi: 10.1104/pp.96.4.1086

Initiation of the Degradation of the Soybean Kunitz and Bowman-Birk Trypsin Inhibitors by a Cysteine Protease 1

Gregory Papastoitsis 1,2, Karl A Wilson 1
PMCID: PMC1080897  PMID: 16668302

Abstract

Protease K1 activity initiates the degradation of the Kunitz soybean trypsin inhibitor (KSTI) during germination and early seedling growth. This enzyme was purified nearly 1300-fold from the cotyledons of 4-day-old soybean (Glycine max [L.] Merrill) seedlings. Protease K1 is a cysteine protease with a molecular weight of approximately 29,000. It cleaves the native form of KSTI, Tia, to Tiam, the same modified form observed in vivo. In addition to attacking KSTI, protease K1 is also active toward the major Bowman-Birk soybean trypsin inhibitor, as well as the α, α′, and β subunits of soybean β-conglycinin. The properties and temporal variation of protease K1 during germination indicate that it is responsible for initiating the degradation of both KSTI and Bowman-Birk soybean trypsin inhibitor in the soybean cotyledon.

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Selected References

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

  1. BEERS R. F., Jr, SIZER I. W. A spectrophotometric method for measuring the breakdown of hydrogen peroxide by catalase. J Biol Chem. 1952 Mar;195(1):133–140. [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. Catsimpoolas N., Funk S. K., Wang J., Kenney J. Isoelectric fractionation and some properties of a protease from soyabean seeds. J Sci Food Agric. 1971 Feb;22(2):79–82. doi: 10.1002/jsfa.2740220209. [DOI] [PubMed] [Google Scholar]
  4. 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]
  5. Earnshaw J. C., Crawford G. E. Viscoelastic relaxation of bilayer lipid membranes: II. Temperature dependence of relaxation time. Biophys J. 1989 May;55(5):1017–1021. doi: 10.1016/S0006-3495(89)82900-5. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Hara-Nishimura I., Nishimura M., Matsubara H., Akazawa T. Suborganellar localization of proteinase catalyzing the limited hydrolysis of pumpkin globulin. Plant Physiol. 1982 Sep;70(3):699–703. doi: 10.1104/pp.70.3.699. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  8. Mitsuhashi W., Koshiba T., Minamikawa T. Separation and Characterization of Two Endopeptidases from Cotyledons of Germinating Vigna mungo Seeds. Plant Physiol. 1986 Mar;80(3):628–634. doi: 10.1104/pp.80.3.628. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Tan-Wilson A. L., Rightmire B. R., Wilson K. A. Different Rates of Metabolism of Soybean Proteinase Inhibitors during Germination. Plant Physiol. 1982 Aug;70(2):493–497. doi: 10.1104/pp.70.2.493. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Wilson K. A., Chen J. C. Amino Acid Sequence of Mung Bean Trypsin Inhibitor and Its Modified Forms Appearing during Germination. Plant Physiol. 1983 Feb;71(2):341–349. doi: 10.1104/pp.71.2.341. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Wilson K. A., Papastoitsis G., Hartl P., Tan-Wilson A. L. Survey of the Proteolytic Activities Degrading the Kunitz Trypsin Inhibitor and Glycinin in Germinating Soybeans (Glycine max). Plant Physiol. 1988 Oct;88(2):355–360. doi: 10.1104/pp.88.2.355. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Wilson K. A., Rightmire B. R., Chen J. C., Tan-Wilson A. L. Differential Proteolysis of Glycinin and beta-Conglycinin Polypeptides during Soybean Germination and Seedling Growth. Plant Physiol. 1986 Sep;82(1):71–76. doi: 10.1104/pp.82.1.71. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Wilson K. A., Tan-Wilson A. L. Characterization of the Proteinase that Initiates the Degradation of the Trypsin Inhibitor in Germinating Mung Beans (Vigna radiata). Plant Physiol. 1987 May;84(1):93–98. doi: 10.1104/pp.84.1.93. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Wilson K. A. The proteolysis of trypsin inhibitors in legume seeds. Crit Rev Biotechnol. 1988;8(3):197–216. doi: 10.3109/07388558809147557. [DOI] [PubMed] [Google Scholar]
  15. Wray W., Boulikas T., Wray V. P., Hancock R. Silver staining of proteins in polyacrylamide gels. Anal Biochem. 1981 Nov 15;118(1):197–203. doi: 10.1016/0003-2697(81)90179-2. [DOI] [PubMed] [Google Scholar]

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