Characterization of [3H]palmitate- and [3H]ethanolamine-labelled proteins in the multicellular parasitic trematode Schistosoma mansoni.

P. M. Wiest, E. J. Tisdale, W. L. Roberts, T. L. Rosenberry, A. A. Mahmoud, A. M. Tartakoff

Research output: Contribution to journalArticle

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Abstract

Biosynthetic labelling experiments with cercariae and schistosomula of the multicellular parasitic trematode Schistosoma mansoni were performed to determine whether [3H]palmitate or [3H]ethanolamine was incorporated into proteins. Parasites incorporated [3H]palmitate into numerous proteins, as judged by SDS/polyacrylamide-gel electrophoresis and fluorography. The radiolabel was resistant to extraction with chloroform, but sensitive to alkaline hydrolysis, indicating the presence of an ester bond. Further investigation of the major 22 kDa [3H]palmitate-labelled species showed that the label could be recovered in a Pronase fragment which bound detergent and had an apparent molecular mass of 1200 Da as determined by gel filtration on Sephadex LH-20. Schistosomula incubated with [3H]ethanolamine for up to 24 h incorporated this precursor into several proteins; labelled Pronase fragments recovered from the three most intensely labelled proteins were hydrophilic and had a molecular mass of approx. 200 Da. Furthermore, reductive methylation of such fragments showed that the [3H]ethanolamine bears a free amino group, indicating the lack of an amide linkage. We also evaluated the effect of phosphatidylinositol-specific phospholipase C from Staphylococcus aureus: [3H]palmitate-labelled proteins of schistosomula and surface-iodinated proteins were resistant to hydrolysis with this enzyme. In conclusion, [3H]palmitate and [3H]ethanolamine are incorporated into distinct proteins of cercariae and schistosomula which do not bear glycophospholipid anchors. The [3H]ethanolamine-labelled proteins represent a novel variety of protein modification.

Original languageEnglish (US)
Pages (from-to)419-426
Number of pages8
JournalBiochemical Journal
Volume254
Issue number2
StatePublished - Sep 1 1988
Externally publishedYes

Fingerprint

Ethanolamine
Schistosoma mansoni
Palmitates
Proteins
Cercaria
Pronase
Molecular mass
Photofluorography
Hydrolysis
Phosphoinositide Phospholipase C
Methylation
Chloroform
Electrophoresis
Anchors
Amides
Detergents
Labeling
Gel Chromatography
Staphylococcus aureus
Labels

ASJC Scopus subject areas

  • Biochemistry

Cite this

Wiest, P. M., Tisdale, E. J., Roberts, W. L., Rosenberry, T. L., Mahmoud, A. A., & Tartakoff, A. M. (1988). Characterization of [3H]palmitate- and [3H]ethanolamine-labelled proteins in the multicellular parasitic trematode Schistosoma mansoni. Biochemical Journal, 254(2), 419-426.

Characterization of [3H]palmitate- and [3H]ethanolamine-labelled proteins in the multicellular parasitic trematode Schistosoma mansoni. / Wiest, P. M.; Tisdale, E. J.; Roberts, W. L.; Rosenberry, T. L.; Mahmoud, A. A.; Tartakoff, A. M.

In: Biochemical Journal, Vol. 254, No. 2, 01.09.1988, p. 419-426.

Research output: Contribution to journalArticle

Wiest, PM, Tisdale, EJ, Roberts, WL, Rosenberry, TL, Mahmoud, AA & Tartakoff, AM 1988, 'Characterization of [3H]palmitate- and [3H]ethanolamine-labelled proteins in the multicellular parasitic trematode Schistosoma mansoni.', Biochemical Journal, vol. 254, no. 2, pp. 419-426.
Wiest PM, Tisdale EJ, Roberts WL, Rosenberry TL, Mahmoud AA, Tartakoff AM. Characterization of [3H]palmitate- and [3H]ethanolamine-labelled proteins in the multicellular parasitic trematode Schistosoma mansoni. Biochemical Journal. 1988 Sep 1;254(2):419-426.
Wiest, P. M. ; Tisdale, E. J. ; Roberts, W. L. ; Rosenberry, T. L. ; Mahmoud, A. A. ; Tartakoff, A. M. / Characterization of [3H]palmitate- and [3H]ethanolamine-labelled proteins in the multicellular parasitic trematode Schistosoma mansoni. In: Biochemical Journal. 1988 ; Vol. 254, No. 2. pp. 419-426.
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