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.
Hintz
M
M
Biochemisches Institut am Klinikum, Giessen, Germany.
Hirzmann
J
J
Hobom
G
G
Linder
D
D
Lottspeich
F
F
Schott
H H
HH
Conraths
F J
FJ
Zahner
H
H
Stirm
S
S
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