| Id |
Subject |
Object |
Predicate |
Lexical cue |
| TextSentencer_T1 |
0-116 |
Sentence |
denotes |
Requirement for a different hydrophobic moiety and reliable chromogenic substrate for endo-type glycosylceramidases. |
| T1 |
0-116 |
Sentence |
denotes |
Requirement for a different hydrophobic moiety and reliable chromogenic substrate for endo-type glycosylceramidases. |
| T1 |
0-116 |
Sentence |
denotes |
Requirement for a different hydrophobic moiety and reliable chromogenic substrate for endo-type glycosylceramidases. |
| TextSentencer_T2 |
117-285 |
Sentence |
denotes |
A series of synthetic lactosides with aglycones that differed in length and structure were used to determine the substrate specificity of endo-type glycosylceramidases. |
| T2 |
117-285 |
Sentence |
denotes |
A series of synthetic lactosides with aglycones that differed in length and structure were used to determine the substrate specificity of endo-type glycosylceramidases. |
| T2 |
117-285 |
Sentence |
denotes |
A series of synthetic lactosides with aglycones that differed in length and structure were used to determine the substrate specificity of endo-type glycosylceramidases. |
| TextSentencer_T3 |
286-410 |
Sentence |
denotes |
Endoglycoceramidases (EGCase) from bacteria preferred lactosides with an acylamide structure over simple n-alkyl lactosides. |
| T3 |
286-410 |
Sentence |
denotes |
Endoglycoceramidases (EGCase) from bacteria preferred lactosides with an acylamide structure over simple n-alkyl lactosides. |
| T3 |
286-410 |
Sentence |
denotes |
Endoglycoceramidases (EGCase) from bacteria preferred lactosides with an acylamide structure over simple n-alkyl lactosides. |
| TextSentencer_T4 |
411-479 |
Sentence |
denotes |
While ceramide glycanase (CGase) from leech did not show preference. |
| T4 |
411-479 |
Sentence |
denotes |
While ceramide glycanase (CGase) from leech did not show preference. |
| T4 |
411-479 |
Sentence |
denotes |
While ceramide glycanase (CGase) from leech did not show preference. |
| TextSentencer_T5 |
480-705 |
Sentence |
denotes |
N -Acylaminoethyl beta-lactosides and n -alkyl lactosides were substrates for both EGCase and CGase, but N-acylaminobutyl beta-lactosides, whose acylamide residue differs from that in ceramide, were not hydrolyzed by EGCases. |
| T5 |
480-705 |
Sentence |
denotes |
N -Acylaminoethyl beta-lactosides and n -alkyl lactosides were substrates for both EGCase and CGase, but N-acylaminobutyl beta-lactosides, whose acylamide residue differs from that in ceramide, were not hydrolyzed by EGCases. |
| T5 |
480-705 |
Sentence |
denotes |
N -Acylaminoethyl beta-lactosides and n -alkyl lactosides were substrates for both EGCase and CGase, but N-acylaminobutyl beta-lactosides, whose acylamide residue differs from that in ceramide, were not hydrolyzed by EGCases. |
| TextSentencer_T6 |
706-853 |
Sentence |
denotes |
Thus, EGCases, but not CGase, appear to require an N-acyl group at the same position as that of intact glycosphingolipid for substrate recognition. |
| T6 |
706-853 |
Sentence |
denotes |
Thus, EGCases, but not CGase, appear to require an N-acyl group at the same position as that of intact glycosphingolipid for substrate recognition. |
| T6 |
706-853 |
Sentence |
denotes |
Thus, EGCases, but not CGase, appear to require an N-acyl group at the same position as that of intact glycosphingolipid for substrate recognition. |
| TextSentencer_T7 |
854-1062 |
Sentence |
denotes |
A p-nitrophenyl lactoside derivative possessing an N-acyl chain was degraded by both EGCases and CGase and this chromogenic substrate may be an alternative substrate for endo-type glycosylceramidase activity. |
| T7 |
854-1062 |
Sentence |
denotes |
A p-nitrophenyl lactoside derivative possessing an N-acyl chain was degraded by both EGCases and CGase and this chromogenic substrate may be an alternative substrate for endo-type glycosylceramidase activity. |
| T7 |
854-1062 |
Sentence |
denotes |
A p-nitrophenyl lactoside derivative possessing an N-acyl chain was degraded by both EGCases and CGase and this chromogenic substrate may be an alternative substrate for endo-type glycosylceramidase activity. |
| TextSentencer_T8 |
1063-1168 |
Sentence |
denotes |
Km of the chromogenic lactoside for CGase and Rhodococcus EGCase were 28 microM and 2.9 mM, respectively. |
| T8 |
1063-1168 |
Sentence |
denotes |
Km of the chromogenic lactoside for CGase and Rhodococcus EGCase were 28 microM and 2.9 mM, respectively. |
| T8 |
1063-1168 |
Sentence |
denotes |
Km of the chromogenic lactoside for CGase and Rhodococcus EGCase were 28 microM and 2.9 mM, respectively. |