Introduction: Proteinaceous inhibitors of animal trypsin occur naturally as isoforms in seeds and some are of interest as antinutritional or anti-pest agents.
Objective: To establish a simplified electrophorectic, in-gel method for rapid and direct detection of trypsin isoinhibitors present in crude plant extracts that are particularly suitable for many studies including rapid evaluation of cultivars.
Methodology: Azoalbumin (3%, w/v) is immobilised in 7.5% polyacrylamide gels before electrophoresis under non-denaturing conditions.
Results: This improved method eliminates the need for both time-consuming and labourious staining and destaining or renaturation steps.
Conclusion: Immobilised azoalbumin in polyacrylamide gels, run under non-denaturing electrophoresis conditions, can be used to assist rapid evaluation of trypsin isoinhibitors in numerous crude plant extracts.
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http://dx.doi.org/10.1002/pca.1290 | DOI Listing |
Biochem J
March 2021
Center for Pharmacology and Physiology, Medical University of Vienna, Schwarzspanierstr. 17, 1090 Vienna, Austria.
Bowman-Birk inhibitors (BBIs) are plant-derived serine proteinase inhibitors. Endogenously, they function as defense molecules against pathogens and insects, but they also have been explored for applications in cancer treatment and inflammatory disorders. Here, we isolated 15 novel BBIs from the bulb of Hyacinthus orientalis (termed HOSPIs).
View Article and Find Full Text PDFFront Plant Sci
March 2020
Department of Biotechnology and Bioinformatics, School of Life Sciences, University of Hyderabad, Hyderabad, India.
Food Funct
September 2019
Estación Experimental del Zaidín (EEZ, CSIC), Profesor Albareda 1, Granada 18008, Spain.
Naturally-occurring serine protease inhibitors of the Bowman-Birk family, particularly abundant in legume seeds, exert their potential chemopreventive and/or therapeutic properties via protease inhibition. Processing of legume seeds, including soybeans, has been proposed as a major cause for their loss of bioactivity due to glycation. In order to assess how glycation affected the protease inhibitory activities of major soybean Bowman-Birk isoinhibitors (BBI) and their antiproliferative properties, IBB1 and IBBD2 were purified and subjected to glycation under controlled conditions using glucose at high temperature.
View Article and Find Full Text PDFPhytochemistry
March 2019
Department of Biotechnology & Bioinformatics, School of Life Sciences, University of Hyderabad, Hyderabad, 500 046, Telangana, India. Electronic address:
Rhynchosia sublobata, a wild relative of pigeonpea, possesses defensive proteinase/protease inhibitors (PIs). Characterization of trypsin specific PIs (RsPI) separated from seeds by column chromatography using 2-D gel electrophoresis and Edman degradation method identified R. sublobata possessed both Bowman-Birk isoinhibitors (RsBBI) and Kunitz isoinhibitors (RsKI).
View Article and Find Full Text PDFFront Physiol
September 2016
Department of Biotechnology and Bioinformatics, School of Life Sciences, University of Hyderabad Hyderabad, India.
Proteinase inhibitors (PIs) are natural defense proteins of plants found to be active against gut proteases of various insects. A pigeonpea wild relative Cajanus platycarpus was identified as a source of resistance against Helicoverpa armigera, a most devastating pest of several crops including pigeonpea. In the light of earlier studies, trypsin-specific PIs (CpPI 63) were purified from mature dry seeds of C.
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