Removal of ester-bound fatty acyl residues from Salmonella lipopolysaccharide by enzyme preparations from Acanthamoeba castellanii
✍ Scribed by Wincenty Drozanski; Abd El-Halim A. Moustafa; Otto Lüderitz; Otto Westphal
- Book ID
- 102993574
- Publisher
- Elsevier Science
- Year
- 1988
- Tongue
- English
- Weight
- 531 KB
- Volume
- 178
- Category
- Article
- ISSN
- 0008-6215
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✦ Synopsis
Three enzyme preparations (EIa, EIIa, and EIII), which exhibited fatty acyl esterase activity towards p-nitrophenyl laurate and towards the lipopolysaccharide from Salmonella minnesotu R4, were obtained from a cell-free lysate of Acanthamoeba castellanii. In the presence of Triton X-100, EIa and EIIa cleaved all ester-bound fatty acids from the lipopolysaccharide, and EIII cleaved non-and 2-hydroxylated fatty acids, but not ester-(and amide-)bound 3-hydroxymyristic acid. The content of heptose, 3-deoxy-2-octulosonic acid, glucosamine, and phosphate in the degraded preparations was unchanged, although phosphatase and Nacetyl-P-D-glucosaminidase activity was detectable in the enzyme preparations when tested with the respective p-nitrophenyl substrates.