Pub. Date : 1992 Nov 23
PMID : 1329966
9 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | Glycolipid-anchored acetylcholinesterases from rabbit lymphocytes and erythrocytes differ in their sensitivity to phosphatidylinositol-specific phospholipase C. The type of membrane association of acetylcholinesterase (AChE, EC 3.1.1.7) was studied in rabbit lymphocytes and erythrocytes. | Glycolipids | ACE-1 | Oryctolagus cuniculus |
| 2 | Glycolipid-anchored acetylcholinesterases from rabbit lymphocytes and erythrocytes differ in their sensitivity to phosphatidylinositol-specific phospholipase C. The type of membrane association of acetylcholinesterase (AChE, EC 3.1.1.7) was studied in rabbit lymphocytes and erythrocytes. | Glycolipids | ACE-1 | Oryctolagus cuniculus |
| 3 | Glycolipid-anchored acetylcholinesterases from rabbit lymphocytes and erythrocytes differ in their sensitivity to phosphatidylinositol-specific phospholipase C. The type of membrane association of acetylcholinesterase (AChE, EC 3.1.1.7) was studied in rabbit lymphocytes and erythrocytes. | Phosphatidylinositols | ACE-1 | Oryctolagus cuniculus |
| 4 | Glycolipid-anchored acetylcholinesterases from rabbit lymphocytes and erythrocytes differ in their sensitivity to phosphatidylinositol-specific phospholipase C. The type of membrane association of acetylcholinesterase (AChE, EC 3.1.1.7) was studied in rabbit lymphocytes and erythrocytes. | Phosphatidylinositols | ACE-1 | Oryctolagus cuniculus |
| 5 | In both cases, the unique AChE molecular form was an amphiphilic dimer (referred to as G2a) anchored in the membrane by a glycosylphosphatidylinositol. | Glycosylphosphatidylinositols | ACE-1 | Oryctolagus cuniculus |
| 6 | In lymphocytes, G2a AChE was directly converted into its hydrophilic G2h counterpart by a treatment with Bacillus thuringiensis phosphatidylinositol-phospholipase C (PI-PLC, EC 3.1.4.10). | g2h | ACE-1 | Oryctolagus cuniculus |
| 7 | In erythrocytes, AChE was resistant to PI-PLC but was rendered sensitive by a prior deacylation with alkaline hydroxylamine. | alkaline hydroxylamine | ACE-1 | Oryctolagus cuniculus |
| 8 | This observation suggests that, as previously reported for human erythrocyte AChE, an acylation of the inositol ring in the glycolipid anchor of rabbit erythrocyte AChE (that does not occur in lymphocytes) prevents the cleavage. | Inositol | ACE-1 | Oryctolagus cuniculus |
| 9 | This observation suggests that, as previously reported for human erythrocyte AChE, an acylation of the inositol ring in the glycolipid anchor of rabbit erythrocyte AChE (that does not occur in lymphocytes) prevents the cleavage. | Glycolipids | ACE-1 | Oryctolagus cuniculus |