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Synthesis of ethanolamine phosphoglycerides by human platelets.
| Content Provider | Semantic Scholar |
|---|---|
| Author | Call, F. L. Rubert, M. W. |
| Copyright Year | 1975 |
| Abstract | Platelet homogenates contain an ethanolaminephosphotransferase (EC 2.7.8.1) that catalyzes the synthesis of ethanolamine phosphoglycerides from cytidine-5'-diphosphate ethanolamine and 1-radyl-2-acyl-sn-glycerols. The enzyme is particulate-bound and requires Mn2+ and bile salts for optimal activity. The apparent Km of the enzyme for cytidine-5'-diphosphate ethanolamine is 1.6 X 10(-5) M when the concentration of 1,2-diacyl-sn-glycerols is 8.8 X 10(-4) M. The pH optimum is 8.5 in Tris-HCl or glycine-NaOH buffer. The activity of the enzyme in platelets from normal subjects is 0.24-0.34 nmole/min/mg of protein. |
| File Format | PDF HTM / HTML |
| PubMed reference number | 240899 |
| Journal | Medline |
| Volume Number | 16 |
| Issue Number | 5 |
| Alternate Webpage(s) | http://www.jlr.org/content/16/5/352.full.pdf |
| Journal | Journal of lipid research |
| Language | English |
| Access Restriction | Open |
| Content Type | Text |
| Resource Type | Article |