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Degradation of the endosperm cell walls of Lactuca sativa L., cv. grand rapids in relation to the mobilisation of proteins and the production of hydrolytic enzymes in the axis, cotyledons and endosperm

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Abstract

The timing of changes in total nitrogen and soluble amino nitrogen content, and in the activities of proteinase (pH 7.0), isocitrate lyase, catalase, phytase, phosphatase (pH 5.0), α-galactosidase and β-mannosidase were studied in extracts from the cotyledons, axis and endosperms of germinating and germinated light-promoted lettuce seeds. The largest amount of total nitrogen (2.7% seed dry weight) occurs within the cotyledons, as storage protein. As this decreases the total nitrogen content of the axis increases and the soluble amino nitrogen in the cotyledons and axis increases. Proteinase activity in the cotyledons increases coincidentally with the depletion of total nitrogen therein. Enzymes for phytate mobilisation and for gluconeogenesis of hydrolysed lipids increase in activity in the cotyledons as the appropriate stored reserves decline. Beta-mannosidase, an enzyme involved in the hydrolysis of oligo-mannans released by the action of endo-β-mannase on mannan reserves in the endosperm, arises within the cotyledons. This indicates that complete hydrolysis of mannans to the monomer does not occur within the endosperm. Mobilisation of all cotyledon reserves occurs after the endosperm has been degraded, providing further evidence that the endosperm is an early source of food reserves for the growing embryo.

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Abbreviations

HEPES:

N-2-hydroxyethylpiperazine-N′-2-ethanesulphonic acid

EDTA:

ethylenediamine tetraacetic acid disodium salt

TCA:

trichloroacetic acid

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Part 2 of a series, of which the first was published in Planta 139, 1–8 (1978)

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Leung, D.W.M., Reid, J.S.G. & Bewley, J.D. Degradation of the endosperm cell walls of Lactuca sativa L., cv. grand rapids in relation to the mobilisation of proteins and the production of hydrolytic enzymes in the axis, cotyledons and endosperm. Planta 146, 335–341 (1979). https://doi.org/10.1007/BF00387806

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  • DOI: https://doi.org/10.1007/BF00387806

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