Comparison of the amino acid compositions and antigenic properties of spiralins purified from the plasma membranes of different spiroplasmas.
Ann Microbiol (Paris)
; 135A(1): 73-82, 1984.
Article
em En
| MEDLINE
| ID: mdl-6201097
ABSTRACT
Spiralins were purified by agarose-suspension electrophoresis after extraction with detergents from the membranes of the following spiroplasmas Spiroplasma citri C189, S. citri Maroc (R8A2), S. citri Scaph and the honey-bee spiroplasma B88. The four proteins (molecular mass congruent to 26,000 daltons, as determined by sodium dodecyl sulphate-pore gradient electrophoresis) showed very similar amino acid compositions characterized by the absence of methionine and tryptophan and a high polarity index (greater than 49%). When compared with the amino acid composition of S. citri membrane, the four spiralins had little or no histidine, a low content of glycine, leucine, tyrosine, phenylalanine and arginine, and a high content of threonine, alanine and valine. Comparison of the amino acid compositions according to the criteria described by Cornish-Bowden (Anal. Biochem., 1980, 105, 233-238) strongly suggests that all four spiralins are related. A crossed immunoelectrophoretical comparison, however, shows that though the three proteins purified from S. citri strains (serogroup I-1) are antigenically similar, they do not seem to share common epitopes with spiralin from the honey-bee spiroplasma B88 (serogroup I-2).
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Base de dados:
MEDLINE
Assunto principal:
Spiroplasma
/
Proteínas da Membrana Bacteriana Externa
/
Proteínas de Bactérias
/
Aminoácidos
/
Proteínas de Membrana
/
Epitopos
/
Antígenos de Bactérias
Idioma:
En
Ano de publicação:
1984
Tipo de documento:
Article