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Mem. Inst. Oswaldo Cruz ; 91(1): 111-6, Jan.-Feb. 1996. tab
Article in English | LILACS | ID: lil-164146

ABSTRACT

The four dominant outer membrane proteins (46, 38 33 and 28 kDa) were detected by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) in a semi-purified preparation of vesicle membranes of a Neisseria meningitidis (N44/89, B:4:P1.15:P5.5,7) strain isolated in Brazil. The N-terminal amino acid sequence for the 46 kDa and 28 kDa proteins matched that reported by others for class 1 and 5 proteins respectively, whereas the sequence (25 amino acids) for the 38 kDa (class 3) protein was similar to class 1 meningococcal proteins. The sequence for the 33 kDa (class 4) was unique and not homologous to any known protein.


Subject(s)
Amino Acids , Neisseria meningitidis/isolation & purification , Membrane Proteins , Meningitis, Meningococcal
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