Abstract
A dolichol kinase (EC 2.7.1.108) was found in sarcoplasmic reticulum membrame fractions from rat leg muscle. This enzyme specifically required CTP as a phosphoryl donor and relatively little activity was found in the absence of exogenous detergent-suspended dolichol. Unlike other reported dolichol kinases, the kinase from skeletal muscle was activated almost equally well by Ca 2+, Zn 2+, or Mg 2+, but not Mn 2+. No effect of calmodulin was seen. The kinase exhibited a single pH optimum at pH 7–8 in contrast to kinases from certain other tissues. Despite the low level of dolichol present in skeletal muscle, the kinase in the sarcoplasmic reticulum fraction had an activity comparable to that of microsomal preparations from tissues such as brain and liver, which may indicate that skeletal muscle has a high capacity for dolichol phosphorylation and protein glycosylation.
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Schedule a callMore From: Biochimica et Biophysica Acta (BBA)/Lipids and Lipid Metabolism
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