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.
CITATION STYLE
Gustafson, G., & Ryan, C. A. (1977). Disulfide crosslinks and the specificity of protein turnover in plants. Advances in Experimental Medicine and Biology, 86 A, 31–42. https://doi.org/10.1007/978-1-4684-3282-4_2
Mendeley helps you to discover research relevant for your work.