Purification of gibberellic acid-induced lysosomes from wheat aleurone cells.

R. A. Gibson, L. G. Paleg

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Abstract

Using isopycnic density gradient centrifugation, lysosomes were concentrated in a single region of a sucrose-Ficoll gradient (p = 1-10 g cm-3), well separated from most other cell organelles. Gibberellic acid-induced lysosomes were found to be rich in alpha-amylase and protease but not ribonuclease. The lysosomal band also contained a majority of the NADH2-cytochrome c reductase, a marker enzyme for endoplasmic reticulum, found in the gradient. Examination of electron micrographs revealed that a purified band of lyosomes contained at least 3 vesicle types, ranging in size from 0-1 to 0-5 mum. The significance of these findings to proposed mechanisms of action of gibberellic acid is discussed.

LanguageEnglish
Pages413-425
Number of pages13
JournalJournal of Cell Science
Volume22
Issue number2
Publication statusPublished - 1 Nov 1976
Externally publishedYes

ASJC Scopus subject areas

  • Cell Biology

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