The protease resistant surface (PRS) glycoconjugate from Trypanosoma congolense has an inositol-acylated glycosylphosphatidylinositol anchor, containing a significant proportion of myristate at the sn-2 position

Molecular and Biochemical Parasitology

Volumn 171, Issue 1, 2010, Pages 50-54

  Greganova, Eva ^a   Bütikofer, Peter ^a   Acosta Serrano, Alvaro ^b  

^a UNIVERSITY OF BERN   (Switzerland)

^b UNIVERSITY OF GLASGOW   (United Kingdom)

Author keywords

GPI myristoylation; Mass spectrometry; Protease resistant surface molecule; Sialic acid; Trypanosoma congolense

Indexed keywords

ALANINE; CARBOHYDRATE; CYCLINE; GALACTOSE; GLUTAMIC ACID; GLYCEROL; GLYCOSYLPHOSPHATIDYLINOSITOL ANCHORED PROTEIN; LIPID; MYRISTIC ACID; OLEIC ACID; PROTEINASE; SIALIC ACID; SIALIDASE;

ARTICLE; CARBOHYDRATE ANALYSIS; CONJUGATION; CONTROLLED STUDY; EPIMASTIGOTE; LIPID COMPOSITION; MASS SPECTROMETRY; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN PURIFICATION; PROTEIN STRUCTURE; TRYPANOSOMA CONGOLENSE; TSETSE FLY;

CELL MEMBRANE; GALACTOSE; GLYCOCONJUGATES; GLYCOSYLPHOSPHATIDYLINOSITOLS; MASS SPECTROMETRY; MYRISTIC ACID; N-ACETYLNEURAMINIC ACID; OLEIC ACID; PROTOZOAN PROTEINS; TRYPANOSOMA CONGOLENSE;

GLOSSINA (GENUS); TRYPANOSOMA CONGOLENSE;

EID: 77649337894     PISSN: 01666851     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molbiopara.2010.02.001     Document Type: Article

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