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  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 32 (1974), S. 0 
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The activities of trypsin inhibitors and Aspergillus-proteinase inhibitors have been assayed in barley embryos germinating in different conditions.The Aspergillus-proteinase inhibitor activity increased about 20-fold during 6 days at 20°C both in separated embryos germinating on nutrient agar and in the embryos of undissected grains germinating on agar with or without mineral salts. Significant inhibitor activity was also present in root tips at later stages of vegetative growth. Whether any changes occurred in the molecular weight distribution of the inhibitors present in the seedlings was studied by gel filtration on Sephadex G-75; only minor changes were observed.The trypsin inhibitor activity per seedling remained roughly constant in all cultures. In gel filtration experiments all the activity appeared to be due to the inhibitor species present in resting embryos.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 39 (1977), S. 0 
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Inhibitors of chymotrypsin and the alkaline proteinase of Aspergillus oryzae were present in the shoots of barley seedlings and weak activities were also detected in the shoot tops of 6-week-old plants. Treatments which induce inhibitor formation in tomato and potato leaves had no effect when tested on mature leaves, seedlings, or young tillers of barley.Fractionation experiments with isoelectric focusing showed that the barley leaves contained several proteinase inhibitors acting on both chymotrypsin and the Aspergillus proteinase, and one inhibitor which acted only on the Aspergillus enzyme. All of these inhibitors were different from the five Aspergillus proteinase inhibitors which are abundant in the endosperm of resting seeds. Two chymotrypsin inhibitors with weaker activity on the Aspergillus proteinase were present in rootlets and also in embryos of resting seeds. These inhibitors were different from both the endospermal inhibitors and the inhibitors present in young leaves.
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  • 3
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 29 (1973), S. 0 
    ISSN: 1399-3054
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Assays have been made of the activities of trypsin inhibitors and Aspergillus-proteinase inhibitors in developing grains of barley (Hordeum vulgare L.) grown under controlled conditions. Trypsin inhibitor activity appeared early in the development, reaching a near-maximal value 24 days after anthesis, but Aspergillus-proteinase inhibitors were synthesized quite late in the development. A half-maximal value was attained about 25 days subsequent to anthesis. The corresponding half-maximal value for all the proteins synthesized was about 16 days.The trypsin inhibitor present in developing grains appeared to be immunologically identical with the endospermal inhibitor in mature grains.The concentrations of Aspergillus-proteinase inhibitors varied between different cultivars of barley. Moreover, each cultivar displayed an almost linear relationship between inhibitor activity and the increasing content of total protein. Great differences between different cultivars were also observable with regard to trypsin inhibitor activities. However, the activities in each cultivar were constant, regardless of the total protein content.The author is greatly indebted to Dr. Juhani Mikola for many helpful discussions during the course of the work, and for several valuable suggestions in regard to the manuscript. I also wish to thank Mrs. Marja-Leena Niku-Paavola, Lic. Phil., for valuable help in the immunodiffusion experiments, and Miss Outi Karkkainen for skilful technical assistance. This work was supported by grants from the Emil Aaltonen Foundation and from the E. J. Sariola Foundation.
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  • 4
    Publication Date: 1983-01-01
    Print ISSN: 0031-9422
    Electronic ISSN: 1873-3700
    Topics: Biology , Chemistry and Pharmacology
    Published by Elsevier
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