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Updated: Aug 8, 2026

Measuring Gene Expression in Bombarded Barley Aleurone Layers with Increased Throughput
Published on: March 30, 2018
Barley beta-galactosidase: structure, function, heterogeneity, and gene origin
D Triantafillidou1, J G Georgatsos
1Laboratory of Biochemistry, School of Chemistry, Aristotle University of Thessaloniki, Greece.
Abstract:
Barley (Hordeum vulgare) beta-galactosidase is composed of a large (45 kDa) and a small (33 kDa) polypeptide. N-terminal sequencing of the polypeptides and antibody reactivity data place the barley enzyme and heterodimeric plant beta-galactosidases from jack bean, maize, and wheat in family 35 of the glycosyl hydrolases. Sequence analysis indicates the existence of a subfamily of genes coding for polypeptide precursors that are cleaved to produce the two subunits in heterodimeric beta-galactosidases. The heterogeneity of the barley holoenzyme is related, but not restricted, to the N-glycosylation of the small polypeptide. Both polypeptides are essential for the catalytic activity of the enzyme.
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