Litomosoides carinii microfilarial sheaths: partial amino acid sequences of several major polypeptide constituents.
Isolated sheaths from Litomosoides carinii microfilariae were disintegrated by reduction with dithiothreitol and were 14C-carboxymethylated. Five major sheath proteins thus solubilized were purified by size exclusion chromatography and reversed-phase HPLC (rpHPLC). Proteolytic fragments of complete sheaths and of the single sheath proteins were isolated by rpHPLC and were N-terminally sequenced. A library of 27 partial sheath polypeptide sequences was thus established, 21 of which could be assigned to three L. carinii sheath structural genes (shp1,2, and 3/3a) isolated on the basis of this and of previous amino acid sequence information. The remaining peptides document the presence of at least one additional major sheath constituent.
Biochemisches Institut am Klinikum, Giessen, Germany.
M
M
Hintz
J
J
Hirzmann
G
G
Hobom
D
D
Linder
F
F
Lottspeich
H H
HH
Schott
F J
FJ
Conraths
H
H
Zahner
S
S
Stirm
D000595:Amino Acid Sequence; D000818:Animals; D010450:Endopeptidases; D005370:Filarioidea / Q000235:genetics*; D017238:Genes, Helminth; D006023:Glycoproteins / Q000235:genetics / Q000302:isolation & purification; D015801:Helminth Proteins / Q000235:genetics* / Q000302:isolation & purification; D008842:Microfilariae / Q000235:genetics; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010446:Peptide Fragments / Q000235:genetics / Q000302:isolation & purification; D017386:Sequence Homology, Amino Acid; D012995:Solubility
D006023:Glycoproteins; D015801:Helminth Proteins; D010446:Peptide Fragments; C078443:GP22 protein, Litomosoides carinii; D010450:Endopeptidases