| Autor: |
Taguchi H; Department of Natural Science, Kyoto Women's University, Japan., Kosar-Hashemi B, Paal B, Yang N, Armarego WL |
| Jazyk: |
angličtina |
| Zdroj: |
Biological chemistry Hoppe-Seyler [Biol Chem Hoppe Seyler] 1994 May; Vol. 375 (5), pp. 329-34. |
| DOI: |
10.1515/bchm3.1994.375.5.329 |
| Abstrakt: |
The kinetics of inhibition of glyceryl-ether monooxygenase with 6-methyl-5,6,7,8-tetrahydropterin as cofactor (saturating) by the detergent Mega-10 with batyl alcohol and (RS)-3-(1-hexadecyloxy)-2-hydroxypropane-1-phosphocholine as substrates exhibited noncompetitive inhibition with apparent Ki values of 1.74 +/- 0.37 mM and 185 +/- 23 microM, respectively. Inhibition by octadecan-1-ol (with batyl alcohol as substrate in the presence of 2.3 mM Mega-10) was competitive with an apparent Ki value of 765 +/- 80 microM. The critical micelle concentration values of various solutions of Mega-10 were determined and used to show that the active ether-lipid substrates were in micelle form (for a water soluble substrate) or mixed micelle form (for substrates solubilised with Mega-10). |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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