| Id |
Subject |
Object |
Predicate |
Lexical cue |
| T1 |
0-160 |
Sentence |
denotes |
Molecular cloning and functional expression of two members of mouse NeuAcalpha2,3Galbeta1,3GalNAc GalNAcalpha2,6-sialyltransferase family, ST6GalNAc III and IV. |
| T2 |
161-301 |
Sentence |
denotes |
Two cDNA clones encoding NeuAcalpha2,3Galbeta1,3GalNAc GalNAcalpha2, 6-sialyltransferase have been isolated from mouse brain cDNA libraries. |
| T3 |
302-587 |
Sentence |
denotes |
One of the cDNA clones is a homologue of previously reported rat ST6GalNAc III according to the amino acid sequence identity (94.4%) and the substrate specificity of the expressed recombinant enzyme, while the other cDNA clone includes an open reading frame coding for 302 amino acids. |
| T4 |
588-771 |
Sentence |
denotes |
The deduced amino acid sequence is not identical to those of other cloned mouse sialyltransferases, although it shows the highest sequence similarity with mouse ST6GalNAc III (43.0%). |
| T5 |
772-1018 |
Sentence |
denotes |
The expressed soluble recombinant enzyme exhibited activity toward NeuAcalpha2, 3Galbeta1, 3GalNAc, fetuin, and GM1b, while no significant activity was detected toward Galbeta1,3GalNAc or asialofetuin, or the other glycoprotein substrates tested. |
| T6 |
1019-1181 |
Sentence |
denotes |
The sialidase sensitivity of the 14C-sialylated residue of fetuin, which was sialylated by this enzyme with CMP-[14C]NeuAc, was the same as that of ST6GalNAc III. |
| T7 |
1182-1419 |
Sentence |
denotes |
These results indicate that the expressed enzyme is a new type of GalNAcalpha2,6-sialyltransferase, which requires sialic acid residues linked to Galbeta1,3GalNAc residues for its activity; therefore, we designated it mouse ST6GalNAc IV. |
| T8 |
1420-1553 |
Sentence |
denotes |
Although the substrate specificity of this enzyme is similar to that of ST6GalNAc III, ST6GalNAc IV prefers O-glycans to glycolipids. |
| T9 |
1554-1616 |
Sentence |
denotes |
Glycolipids, however, are better substrates for ST6GalNAc III. |
