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- W2495249526 abstract "This chapter discusses the metabolic aspects of dormancy. It is tempting to speculate that the dormant embryo is unable to resume growth as a consequence of a partial inhibition of protein synthesis. This inhibition could be the result of a number of separate and not mutually exclusive factors, such as compartmentation of the proteases and their substrates, the presence of protease inhibitors, and an insufficiency of the protein synthesis machinery. Further, it has ben suggested that some dormancy breaking phenomena may result from the characteristics of the membrane state in relation to temperature. It is possible to employ this concept to propose that low temperatures, which result in the protein body membrane assuming a quasi-crystalline state, cause the injection of extant proteases into the matrix of the protein body. At higher temperatures, with the membrane being in the liquid-crystalline phase, the enzymes may remain dissolved in or strongly associated with the membrane. In this manner, low temperatures could induce the enzymic breakdown of the stored protein, which would thereby provide the amino acids necessary for the de novo protein synthesis required for growth. Many chemicals, such as ethanol, ethyl ether, and chloroform, are all variously reported to break dormancy in some species. The most difficult step in the formulation of any model of seed dormancy is linking the perception of the environment to consequent changes in metabolism. The physicochemical properties of membranes and how they may hold the key to the block to protein synthesis and subsequent germination are likely to be the focus of much future work." @default.
- W2495249526 created "2016-08-23" @default.
- W2495249526 creator A5023732733 @default.
- W2495249526 date "1984-01-01" @default.
- W2495249526 modified "2023-10-02" @default.
- W2495249526 title "Metabolic Aspects of Dormancy" @default.
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- W2495249526 doi "https://doi.org/10.1016/b978-0-12-511902-3.50007-5" @default.
- W2495249526 hasPublicationYear "1984" @default.