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  • Title: Extraction and detergent/lipid activation of dolichol kinase.
    Author: Allen CM, Muth JD, Gildersleeve N.
    Journal: Biochim Biophys Acta; 1982 Jul 20; 712(1):33-41. PubMed ID: 6288110.
    Abstract:
    The CTP-dependent dolichol kinase from bovine liver microsomes was optimally extracted using either 0.5% sodium deoxycholate or 0.5% Triton X-100 containing 0.5 M NH4Cl. All activity was found in the supernatant fraction following high-speed centrifugation. This fraction was depleted of phospholipid (phospholipid remaining, less than 5% of total) by gel chromatography of the 0.5% deoxycholate extract. This partially purified enzyme was maximally activated 9- or 53-fold over controls in the presence of 0.1% deoxycholate or 0.1% Triton X-100, respectively. Stimulation of the kinase was also observed with mixtures of dimyristoylphosphatidylcholine and deoxycholate. The level of stimulation by these mixtures was up to 20-fold higher than that observed in controls having deoxycholate alone. Dimyristoylphosphatidylcholine alone was not stimulatory. A 1:1 molar ratio of Triton X-100 or deoxycholate to dimyristoylphosphatidylcholine was optimal for enzyme activation. The half-maximum velocity of the dephospholipidated enzyme at 1:1 molar ratio of detergent to dimyristoylphosphatidylcholine was obtained at 150 or 550 microM CTP in the presence of deoxycholate or Triton X-100, respectively. It has been observed, therefore, that dolichol kinase may be extracted from liver microsomes, depleted of endogenous phospholipids and activated by specific molar ratios of detergent to phospholipid.
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