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- W2053550185 abstract "Expression of the Gal α 1,3 Gal epitope on membrane glycolipids and glycoproteins is known to vary widely from one tissue to another. In the course of studying the mechanisms underlying this variability, we have isolated from pig cDNA four sequences corresponding to four isoforms of α 1,3 -galactosyltransferase ( α 1,3 GT), the Golgi enzyme that links galactose in α 1,3 on the galactose residue of N-acetyllactosamine. The isoforms differ from each other in the alternative presence of two nucleotide stretches of 36 and 63 base pairs in a segment encoding the stem region of the protein. Stable expression experiments show that all four isoenzymes can confer α -galactosyltransferase activity to HeLa cells, and that they are all located within the Golgi compartment, indicating that variations in length in the stem region do not affect enzyme activity or cellular localization. Analysis of RNA from different pig organs and cells shows quantitative differences between tissues in levels of α 1,3 GT, as well as qualitative differences, the four isoforms being unequally represented in different tissues." @default.
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- W2053550185 date "1997-03-01" @default.
- W2053550185 modified "2023-09-29" @default.
- W2053550185 title "Porcine α1,3-galactosyltransferase: tissue-specific and regulated expression of splicing isoforms" @default.
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- W2053550185 doi "https://doi.org/10.1016/s0167-4889(96)00151-6" @default.
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