The proteinase inhibitors of plants and micro-organisms

@article{Richardson1977ThePI,
  title={The proteinase inhibitors of plants and micro-organisms},
  author={M. Richardson},
  journal={Phytochemistry},
  year={1977},
  volume={16},
  pages={159-169}
}
Abstract Recent (post-1972) advances in our knowledge of the proteinase inhibitors of plants and micro-organisms are reviewed. Details of the specificity, occurrence and distribution of these proteins are summarized, and modern methods for their isolation, purification and assay are discussed. Certain homologies revealed by comparison of the amino acid sequences of several inhibitors are noted. Details of their reactive (inhibitory) sites are tabulated and discussed in relation to the proposed… Expand
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Naturally occurring α-amylase inhibitors: Structure/function relationships
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Two protein inhibitors of the tryptophan synthase inactivating yeast proteinase B were purified from boiled bakers' yeast extract and are very stable in the pH range of 1 to 10, but they are easily destroyed by incubation with proteinase A and, less effectively, withproteinase B. Expand
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TLDR
The cumulative data suggest that inhibitor I is a major depot or interim storage protein and that its existence in any particular tissue is under complex controls by both the internal and external environments of the plants. Expand
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TLDR
Evidence is presented that the PIIF-induced accumulation of Inhibitor I, determined immunologically, is accompanied by the accumulation of other trypsin and chymotrypsin inhibitors, determined enzymatically. Expand
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TLDR
The activities of trypsin inhibitors and Aspergillus-proteinase inhibitors have been assayed in barley embryos germinating in different conditions and all the activity appeared to be due to the inhibitor species present in resting embryos. Expand
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TLDR
An inhibitor affecting subtilisin was isolated from barley by extraction with 1% sodium chloride, fractionation with ammonium sulfate, chromatography on CM- and DEAE-cellulose columns, and gel filtration on Sephadex G-100, and appears to be distinct from the barley microbial proteinase isoinhibitors reported by Mikola and Suolinna in respect of most of its physiochemical and inhibitory properties. Expand
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