Alliin lyase localication in bundle sheaths of the garlic clove (Allium sativum).
1994
Ellmore G.S. | Feldberg R.S.
The enzyme alliin lyase (E.C. 4.4.1.4) catalyzes formation of allicin, the parent of several sulfur-containing compounds responsible for flavor, odor, and pharmacological properties of garlic (Allium sativum). Alliin lyase is a major product of the storage bud (clove), accounting for 10% of its total protein. Accumulation of this protein was characterized by locating alliin lyase deposits within the clove. Paraffin sections stained for general protein using aniline blue-black reveal dense deposits within parenchymatous bundle sheaths. Deposits are most pronounced around phloem. Remaining storage parenchyma, not in contact with bundles, appears structurally uniform, with some protein accumulating in cells near the outer surface of the clove. In freehand sections of unfixed cloves, bundle sheath cells are the only ones to show green autofluorescence when excited by blue light. Such fluorescence is consistent with the presence of pyridoxal phosphate cofactor of alliin lyase. An alliin lyase activity stain, based on detecting aminocrotonate-generating enzymes, shows activity to be restricted to bundle sheath cells in fresh material. Finally, enrichment of alliin lyase in bundle sheaths is shown by immunocytochemical staining of these areas using a polyclonal antibody generated against purified enzyme. Alliin lyase concentrates in bundle sheaths, while little if any occurs in storage mesophyll not in contact with vascular bundles. Deposits in the cloves may reflect the enzyme's role in protecting underground storage buds from decay and predation. Positioning near the phloem suggests that alliin lyase, or compounds related to its metabolism, may be translocated to and from the clove during development.
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