| Id |
Subject |
Object |
Predicate |
Lexical cue |
| T1 |
0-90 |
Sentence |
denotes |
Human neuraminidases have reduced activity towards modified sialic acids on glycoproteins. |
| T2 |
91-224 |
Sentence |
denotes |
Multiple levels of diversity in sialic acid presentation can influence the substrate activity of sialosides for glycoside hydrolases. |
| T3 |
225-380 |
Sentence |
denotes |
Few reports have investigated the specificity of human neuraminidase (hNEU) activity towards modified sialic acid residues that can occur on glycoproteins. |
| T4 |
381-571 |
Sentence |
denotes |
Previously, we evaluated hNEU activity towards 9-O-acetylated sialic acid in glycolipid substrates and found that hNEU generally discriminated against 9-O-acetylated sialic acid over Neu5Ac. |
| T5 |
572-744 |
Sentence |
denotes |
Here, we have investigated the substrate specificity of hNEU enzymes for a glycoprotein substrate (bovine submaxillary mucin) containing 9-O-acetylated and Neu5Gc residues. |
| T6 |
745-915 |
Sentence |
denotes |
Using this model substrate, we observe a general trend for hNEU tolerance of Neu5Ac > Neu5Gc ≫ Neu5,9Ac2, consistent with our previous results with glycolipid substrates. |
| T7 |
916-1093 |
Sentence |
denotes |
These results expand our understanding of hNEU enzyme specificity and suggest that naturally occurring modifications of sialic acids can play a role in regulating hNEU activity. |
