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- W3023770789 endingPage "370" @default.
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- W3023770789 abstract "This chapter discusses proteinase inhibitors. Proteinase inhibitors found in plants are typically polypeptides and proteins composed entirely of L-amino acids linked through peptide bonds. They generally contain high percentages of half-cystine residues, present as disulfide cross-links, and it is not uncommon for inhibitors to have one half-cystine for every 8–10 amino acid residues. Plant inhibitors are typically low in or devoid of methionine, histidine, and tryptophan but are often rich in aspartic acid, glutamic acid, serine, and lysine residues. No plant proteinase inhibitor has yet been identified as a glycoprotein. This contrasts with the situation in animals, in which several glycoprotein proteinase inhibitors occur. Serine proteinase inhibitors are distributed throughout plants and are found primarily in storage tissues, such as seeds and tubers, where they often represent several percent of the total proteins. Serine proteinase inhibitors also occur in other vegetative tissues but are generally present in lower concentrations than in storage organs. It is not uncommon to find several inhibitor species in a single tissue that are cumulatively specific for a wide spectrum of serine proteinases with both animal and microbial origins." @default.
- W3023770789 created "2020-05-13" @default.
- W3023770789 creator A5037952095 @default.
- W3023770789 date "1981-01-01" @default.
- W3023770789 modified "2023-10-18" @default.
- W3023770789 title "Proteinase Inhibitors" @default.
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