grain_icon  Literature Home |  Rice Genetics Newsletters |  Tutorial |  FAQ
Find:
E.g., Wessler, regeneration, PubMed ID 17578919.

expand all sections collapse all sections  Reference "Barley beta-galactosidase: structure, function, heterogeneity, and gene origin"
Reference ID 8787
Title Barley beta-galactosidase: structure, function, heterogeneity, and gene origin
Source Journal of protein chemistry, 2001, vol. 20, pp. 551-562
Authors (2)
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.
toggle section  Database Cross-References (1)
toggle section  Proteins (1)
box  Markers (0)
box  QTL (0)
box  Genes (0)
toggle section  Ontologies (2)
box  Map Sets (0)
box  Diversity Experiments (0)

Please note:
To request reprints, please contact the authors or the source/journal website. Due to copyright issues Gramene does not distribute reprints.