Learn More
Oligosaccharyltransferase solubilized by Nonidet P-40 was found to have a highly specific lipid requirement which is consistent with the lability of the enzyme when removed from its membrane association. Enzyme activity as measured by the N-glycosylation of a hexapeptide acceptor was greatly stimulated and stabilized by phosphatidylcholine (PC) while other(More)
The hydrolytic and transphosphatidylation activities of rat brain microsomal phospholipase D were highly latent in the absence of an appropriate activator. The most suitable surfactants for this activation were oleate and palmitoleate. Besides the bile acids and unsaturated fatty acids, other naturally occurring surfactants, such as lysophospholipids,(More)
An axolemma-enriched fraction prepared from a purified myelinated axon fraction isolated from rat CNS was found to contain phospholipase D at a specific activity similar to that of a microsomal fraction isolated from whole brain. There was a concomitant threefold enrichment in the specific activity of phospholipase D and acetylcholinesterase in the(More)
Endo-beta-N-acetylglucosaminidase H (endo H) was found to bring about the complete hydrolysis of dolichyl pyrophosphoryl oligosaccharides. Both glycosylated and unglucosylated polymannose oligosaccharides were released by the enzyme through cleavage of the di-N-acetylchitobiose sequence. The action of the endo H on the oligosaccharide-lipids was facilitated(More)
Phosphatidylglycerol formation by a transfer of the phosphatidyl moiety of phosphatidylcholine to free glycerol was demonstrated in rat brain preparations. Identification of the product as phosphatidylglycerol was accomplished by chromatography, chemical derivatization, and enzymatic hydrolysis. The optimum pH for the reaction was 6.0 with an apparent Km(More)
  • 1