Publication | Open Access
The sequence of the mouse 14 kDa <i>β</i>-galactoside-binding lectin and evidence for its synthesis on free cytoplasmic ribosomes
64
Citations
24
References
1989
Year
GlycobiologyImmunologyMolecular BiologyPathologyMouse 14Chicken 14Cellular PhysiologyTumor BiologyProtein SynthesisProtein ExpressionFree Cytoplasmic RibosomesProteomicsGlycosylationProtein FunctionGene ExpressionCell BiologyProtein BiosynthesisNatural SciencesCellular StructureCellular BiochemistryBound PolyribosomesMedicineCarbohydrate-protein Interaction
The partial amino acid sequence of the mouse 14 kDa beta-galactoside-binding lectin has been deduced from cDNA clones corresponding to 86% of the coding sequence and extending to the polyadenylation signal. The deduced amino acid sequence for the murine lectin shows 94% identity with the rat, 89% with human, 86% with bovine and 46% with the chicken 14 kDa lectins. A cDNA probe has been used to analyse genomic DNA and identify a single mRNA of approx. 570 bp in 3T3 fibroblasts, murine erythroleukaemia cells and the murine basement-membrane-secreting Engelbreth-Holm-Swarm tumour. Analysis of free and bound polyribosomes has shown that the lectin message is translated on free cytoplasmic ribosomes.
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