Abstract
Studies of the protein metabolism of detached tomato leaves, hormonally induced to accumulate proteinase inhibitors, have indicated that the state of oxidation of protein-bound half-cystine residues may be a principal parameter affecting in vivo and in vitro stability of leaf proteins. Induced leaves exhibited a general specificity of intracellular protein degradation directed towards the preferential hydrolysis of proteins having free- sulfhydryl residues. Proteins having disulfide cross-linkages, including the proteinase inhibitors, were markedly stable to in vivo degradation, and as a result, accumulated. These results provide a precedence for a cellular protein selection process, resulting from a directed specificity of intracellular protein degradation, which is focused on a particular protein structural parameter.
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© 1977 Plenum Press, New York
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Gustafson, G., Ryan, C.A. (1977). Disulfide Crosslinks and the Specificity of Protein Turnover in Plants. In: Friedman, M. (eds) Protein Crosslinking. Advances in Experimental Medicine and Biology, vol 86A. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-3282-4_2
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DOI: https://doi.org/10.1007/978-1-4684-3282-4_2
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4684-3284-8
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