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Pigment‐associated proteins of Xanthomonas campestris pv. juglandis
Author(s) -
LAWANI L. O.,
ARIRIATU L. E.,
GOVEN A. J.,
KESTER A. S.
Publication year - 1990
Publication title -
plant pathology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.928
H-Index - 85
eISSN - 1365-3059
pISSN - 0032-0862
DOI - 10.1111/j.1365-3059.1990.tb02506.x
Subject(s) - biology , xanthomonas , pigment , ouchterlony double immunodiffusion , polyclonal antibodies , xanthomonas campestris , biochemistry , bacteria , polyacrylamide gel electrophoresis , gel electrophoresis , antiserum , antibody , enzyme , chemistry , gene , genetics , organic chemistry
Two pigment‐protein complexes extracted from the cell membrane of Xanthomonas campestris pv. juglandis with 2% Triton X‐100 were separated from other membrane proteins by electrophoresis on a 10%., non‐denaturing discontinuous polyacrylamide gel. One pigment‐protein complex band was distinct, while the other was diffuse. The apparent M r of the protein from the distinct pigment‐protein band was 16400, while the protein in the diffuse band had an apparent M r of about 45000. The protein in the distinct band consisted of 13 amino acids of which 10% were aromatic, 12% hydroxy, 16% basic, 16% acidic and 46% non‐polar. Polyclonal antibody, against the distinct protein, was used to assay for cross‐reactivity with cell wall and membrane proteins of 23 bacterial species by the Ouchterlony double‐diffusion assay. Seven of the bacteria, representing seven genera, cross‐reacted with the antibody, suggesting that a serologically‐related, pigment‐associated protein is commonly distributed among bacteria and which, unlike the pigment, may limit its use as a chemotaxonomic marker for Xanthomonas .