Id |
Subject |
Object |
Predicate |
Lexical cue |
TextSentencer_T1 |
0-122 |
Sentence |
denotes |
Mutation at histidine 338 of gp91(phox) depletes FAD and affects expression of cytochrome b558 of the human NADPH oxidase. |
TextSentencer_T2 |
123-239 |
Sentence |
denotes |
Defective NADPH oxidase components prevent superoxide (O-2) generation, causing chronic granulomatous disease (CGD). |
TextSentencer_T3 |
240-506 |
Sentence |
denotes |
X-linked CGD patients have mutations in the gene encoding the gp91(phox) subunit of cytochrome b558 and usually lack gp91(phox) protein completely (X91(0)). gp91(phox) is considered to be a flavocytochrome that contains binding sites for NADPH, FAD, as well as heme. |
TextSentencer_T4 |
507-741 |
Sentence |
denotes |
We here report a rare X-linked CGD patient whose neutrophils entirely failed to produce O-2, but presented a diminished expression of gp91(phox) containing about one-third of the heme present in normal individuals by Soret absorption. |
TextSentencer_T5 |
742-812 |
Sentence |
denotes |
Translocation of cytosolic factors p67(phox) and p47(phox) was normal. |
TextSentencer_T6 |
813-960 |
Sentence |
denotes |
However, the FAD content in his neutrophil membranes was as low as that of X91(0) patients, suggesting complete depletion of FAD in his gp91(phox). |
TextSentencer_T7 |
961-1145 |
Sentence |
denotes |
This was in agreement with the finding that a single base substitution (C1024 to T) changed His-338 to Tyr in gp91(phox) in a predicted FAD-binding domain of the flavocytochrome model. |
TextSentencer_T8 |
1146-1367 |
Sentence |
denotes |
The loss of FAD could not be corrected even after addition of reagent FAD or a FAD-rich dehydrogenase fraction isolated from normal neutrophils to the patient's membranes, in a reconstitution in vitro with normal cytosol. |
TextSentencer_T9 |
1368-1483 |
Sentence |
denotes |
These results indicate that His-338 is a very critical residue for FAD incorporation into the NADPH oxidase system. |
TextSentencer_T10 |
1484-1529 |
Sentence |
denotes |
This is the first such mutation found in CGD. |
T1 |
0-122 |
Sentence |
denotes |
Mutation at histidine 338 of gp91(phox) depletes FAD and affects expression of cytochrome b558 of the human NADPH oxidase. |
T2 |
123-239 |
Sentence |
denotes |
Defective NADPH oxidase components prevent superoxide (O-2) generation, causing chronic granulomatous disease (CGD). |
T3 |
240-506 |
Sentence |
denotes |
X-linked CGD patients have mutations in the gene encoding the gp91(phox) subunit of cytochrome b558 and usually lack gp91(phox) protein completely (X91(0)). gp91(phox) is considered to be a flavocytochrome that contains binding sites for NADPH, FAD, as well as heme. |
T4 |
507-741 |
Sentence |
denotes |
We here report a rare X-linked CGD patient whose neutrophils entirely failed to produce O-2, but presented a diminished expression of gp91(phox) containing about one-third of the heme present in normal individuals by Soret absorption. |
T5 |
742-812 |
Sentence |
denotes |
Translocation of cytosolic factors p67(phox) and p47(phox) was normal. |
T6 |
813-960 |
Sentence |
denotes |
However, the FAD content in his neutrophil membranes was as low as that of X91(0) patients, suggesting complete depletion of FAD in his gp91(phox). |
T7 |
961-1145 |
Sentence |
denotes |
This was in agreement with the finding that a single base substitution (C1024 to T) changed His-338 to Tyr in gp91(phox) in a predicted FAD-binding domain of the flavocytochrome model. |
T8 |
1146-1367 |
Sentence |
denotes |
The loss of FAD could not be corrected even after addition of reagent FAD or a FAD-rich dehydrogenase fraction isolated from normal neutrophils to the patient's membranes, in a reconstitution in vitro with normal cytosol. |
T9 |
1368-1483 |
Sentence |
denotes |
These results indicate that His-338 is a very critical residue for FAD incorporation into the NADPH oxidase system. |
T10 |
1484-1529 |
Sentence |
denotes |
This is the first such mutation found in CGD. |