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Activity variation between and within two soybean trypsin inhibitor electrophoretic forms

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Abstract

The Kunitz soybean proteinase inhibitors (SBTI-A2) of 13 soybean pure-lines were examined for variation in antitryptic activity. Extraction of the inhibitor from individual seeds, electrophoresis on polyacrylamide gels, and excision of the inhibitor region from the gels were used to prepare inhibitor samples for assay. Protein content of eluate from the gel portions was determined by absorbance at 280 nm after applying corrections for background absorbance due to gel chemicals. Enzyme inhibition and protein content of the gel eluate were used to calculate the specific activity of the inhibitor obtained from each seed. The coefficient of variation for specific activity measurement was about 12%, and analysis of variance on data from 13 pure-lines showed significant variation in inhibitor activity from genetic and environmental sources. There appeared to be three levels of inhibition averaging 21.9, 29.2, and 39.5 specific activity units.

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Author notes

  1. R. W. Clark

    Present address: Institute of Molecular Biophysics, Florida State University, Tallahassee, Florida

Authors and Affiliations

  1. Department of Agronomy, University of Illinois at Urbana-Champaign, Urbana, Illinois

    R. W. Clark & T. Hymowitz

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  1. R. W. Clark
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  2. T. Hymowitz
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Additional information

This investigation was supported in part by funds from the Illinois Agricultural Experiment Station, National Soybean Processor's Association, and a grant (FR 07030) from the U.S. Public Health Service.

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Clark, R.W., Hymowitz, T. Activity variation between and within two soybean trypsin inhibitor electrophoretic forms. Biochem Genet 6, 169–182 (1972). https://doi.org/10.1007/BF00486401

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  • DOI: https://doi.org/10.1007/BF00486401

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