| Id |
Subject |
Object |
Predicate |
Lexical cue |
| TextSentencer_T1 |
0-186 |
Sentence |
denotes |
Expression of human alpha-l-fucosyltransferase gene homologs in monkey kidney COS cells and modification of potential fucosyltransferase acceptor substrates by an endogenous glycosidase. |
| T1 |
0-186 |
Sentence |
denotes |
Expression of human alpha-l-fucosyltransferase gene homologs in monkey kidney COS cells and modification of potential fucosyltransferase acceptor substrates by an endogenous glycosidase. |
| TextSentencer_T2 |
187-390 |
Sentence |
denotes |
Previous investigations on the monkey kidney COS cell line demonstrated the weak expression of fucosylated cell surface antigens and presence of endogenous fucosyltransferase activities in cell extracts. |
| T2 |
187-390 |
Sentence |
denotes |
Previous investigations on the monkey kidney COS cell line demonstrated the weak expression of fucosylated cell surface antigens and presence of endogenous fucosyltransferase activities in cell extracts. |
| TextSentencer_T3 |
391-539 |
Sentence |
denotes |
RT-PCR analyses have now revealed expression of five homologs of human fucosyltransferase genes, FUT1, FUT4, FUT5, FUT7, and FUT8, in COS cell mRNA. |
| T3 |
391-539 |
Sentence |
denotes |
RT-PCR analyses have now revealed expression of five homologs of human fucosyltransferase genes, FUT1, FUT4, FUT5, FUT7, and FUT8, in COS cell mRNA. |
| TextSentencer_T4 |
540-763 |
Sentence |
denotes |
The enzyme in COS cell extracts acting on unsialylated Type 2 structures is closely similar in its properties to the alpha1,3-fucosyltransferase encoded by human FUT4 gene and does not resemble the product of the FUT5 gene. |
| T4 |
540-763 |
Sentence |
denotes |
The enzyme in COS cell extracts acting on unsialylated Type 2 structures is closely similar in its properties to the alpha1,3-fucosyltransferase encoded by human FUT4 gene and does not resemble the product of the FUT5 gene. |
| TextSentencer_T5 |
764-1054 |
Sentence |
denotes |
Although FUT1 is expressed in the COS cell mRNA, it has not been possible to demonstrate alpha1,2-fucosyltransferase activity in cell extracts but the presence of Le(y) and blood-group A antigenic determinants on the cell surface imply the formation of H-precursor structures at some stage. |
| T5 |
764-1054 |
Sentence |
denotes |
Although FUT1 is expressed in the COS cell mRNA, it has not been possible to demonstrate alpha1,2-fucosyltransferase activity in cell extracts but the presence of Le(y) and blood-group A antigenic determinants on the cell surface imply the formation of H-precursor structures at some stage. |
| TextSentencer_T6 |
1055-1305 |
Sentence |
denotes |
The most strongly expressed fucosyltransferase in the COS cells is the alpha1,6-enzyme transferring fucose to the innermost N -acetylglucosamine unit in N -glycan chains; this enzyme is similar in its properties to the product of the human FUT8 gene. |
| T6 |
1055-1305 |
Sentence |
denotes |
The most strongly expressed fucosyltransferase in the COS cells is the alpha1,6-enzyme transferring fucose to the innermost N -acetylglucosamine unit in N -glycan chains; this enzyme is similar in its properties to the product of the human FUT8 gene. |
| TextSentencer_T7 |
1306-1425 |
Sentence |
denotes |
The enzymes resembling the human FUT4 and FUT8 gene products both had pH optima of 7.0 and were resistant to 10 mM NEM. |
| T7 |
1306-1425 |
Sentence |
denotes |
The enzymes resembling the human FUT4 and FUT8 gene products both had pH optima of 7.0 and were resistant to 10 mM NEM. |
| TextSentencer_T8 |
1426-1523 |
Sentence |
denotes |
The incorporation of fucose into asialo-fetuin was optimal at 5.5 and was inhibited by 10 mM NEM. |
| T8 |
1426-1523 |
Sentence |
denotes |
The incorporation of fucose into asialo-fetuin was optimal at 5.5 and was inhibited by 10 mM NEM. |
| TextSentencer_T9 |
1524-1918 |
Sentence |
denotes |
This result initially suggested the presence of a third fucosyltransferase expressed in the COS cells but we have now shown that triantennary N- glycans with terminal nonreducing galactose units, similar to those present in asialo-fetuin, are modified by a weak endogenous beta-galactosidase in the COS cell extracts and thereby rendered suitable substrates for the alpha1,6-fucosyltransferase. |
| T9 |
1524-1918 |
Sentence |
denotes |
This result initially suggested the presence of a third fucosyltransferase expressed in the COS cells but we have now shown that triantennary N- glycans with terminal nonreducing galactose units, similar to those present in asialo-fetuin, are modified by a weak endogenous beta-galactosidase in the COS cell extracts and thereby rendered suitable substrates for the alpha1,6-fucosyltransferase. |