Purification of dibenzothiophene monooxygenase from a recombinant Escherichia coli
Dibenzothiophene monooxygenase is the first enzyme involved in the degradation of dibenzothiophene. This gene was expressed via the pET28a vector in E. coli and was purified in a single step using affinity chromatography. The protein was purified 39-fold
Adhikari,D.K +4 more
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From biosynthesis to function: the roles of ether lipids in cancer development and treatment. [PDF]
Hu Z +5 more
europepmc +1 more source
Oral Supplementation of an Alkylglycerol Mix Comprising Different Alkyl Chains Effectively Modulates Multiple Endogenous Plasmalogen Species in Mice. [PDF]
Paul S +7 more
europepmc +1 more source
Mechanism of auranofin toxicity: Inhibition of tetrahydrobiopterin metabolism. [PDF]
Yang S +4 more
europepmc +1 more source
From a clinically relevant pain target to a possible analgesic treatment strategy. [PDF]
Latremoliere A.
europepmc +1 more source
1-O-Alkylglycerol Ethers from the Marine Sponge Guitarra abbotti and Their Cytotoxic Activity. [PDF]
Dyshlovoy SA +10 more
europepmc +1 more source
Evolutionary diversity of sphingolipid metabolism proteins in fungi. [PDF]
Płecha M +8 more
europepmc +1 more source
Ether Lipid-Mediated Antioxidant Defense in Alzheimer's Disease. [PDF]
Jové M +7 more
europepmc +1 more source
Genes encoding particulate methane monooxygenase and ammonia monooxygenase share high sequence identity. Degenerate oligonucleotide primers were designed, based on regions of shared amino acid sequence between the 27-kDa polypeptides, which are believed ...
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