Abstract
Major surface polypeptides of Rickettsia japonica migrated to the position of 120, 135, and 145 kDa on sodium dodecyl sulfate-polyacrylamide gel electrophoresis, when the organisms were solubilized at room temperature. Two major bands at the position of 135 and 185 kDa were seen, when the organisms were solubilized by heating before electrophoresis. Heat-denaturation of the 120- and 145-kDa polypeptides in excised gel bands changed their mobility and caused them to migrate to 135- and 185-kDa positions, respectively. Two polypeptides at the 120-kDa position were demonstrated: one is a major heat-modifiable polypeptide and the other a minor heat-stable. Peptide mapping was performed to determine the identity between native and denatured polypeptides.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 575-579 |
| Number of pages | 5 |
| Journal | Microbiology and Immunology |
| Volume | 38 |
| Issue number | 7 |
| State | Published - 1994 |
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Keywords
- Peptide mapping
- Rickettsia japonica
- Spotted fever group rickettsiae
- Surface polypeptides
ASJC Scopus subject areas
- Immunology and Microbiology(all)
- Microbiology
- Microbiology (medical)
Cite this
Analysis of major surface polypeptides of Rickettsia japonica. / Uchiyama, T.; Walker, David; Walker, D. H.
In: Microbiology and Immunology, Vol. 38, No. 7, 1994, p. 575-579.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Analysis of major surface polypeptides of Rickettsia japonica
AU - Uchiyama, T.
AU - Walker, David
AU - Walker, D. H.
PY - 1994
Y1 - 1994
N2 - Major surface polypeptides of Rickettsia japonica migrated to the position of 120, 135, and 145 kDa on sodium dodecyl sulfate-polyacrylamide gel electrophoresis, when the organisms were solubilized at room temperature. Two major bands at the position of 135 and 185 kDa were seen, when the organisms were solubilized by heating before electrophoresis. Heat-denaturation of the 120- and 145-kDa polypeptides in excised gel bands changed their mobility and caused them to migrate to 135- and 185-kDa positions, respectively. Two polypeptides at the 120-kDa position were demonstrated: one is a major heat-modifiable polypeptide and the other a minor heat-stable. Peptide mapping was performed to determine the identity between native and denatured polypeptides.
AB - Major surface polypeptides of Rickettsia japonica migrated to the position of 120, 135, and 145 kDa on sodium dodecyl sulfate-polyacrylamide gel electrophoresis, when the organisms were solubilized at room temperature. Two major bands at the position of 135 and 185 kDa were seen, when the organisms were solubilized by heating before electrophoresis. Heat-denaturation of the 120- and 145-kDa polypeptides in excised gel bands changed their mobility and caused them to migrate to 135- and 185-kDa positions, respectively. Two polypeptides at the 120-kDa position were demonstrated: one is a major heat-modifiable polypeptide and the other a minor heat-stable. Peptide mapping was performed to determine the identity between native and denatured polypeptides.
KW - Peptide mapping
KW - Rickettsia japonica
KW - Spotted fever group rickettsiae
KW - Surface polypeptides
UR - http://www.scopus.com/inward/record.url?scp=0027935288&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0027935288&partnerID=8YFLogxK
M3 - Article
VL - 38
SP - 575
EP - 579
JO - Microbiology and Immunology
JF - Microbiology and Immunology
SN - 0385-5600
IS - 7
ER -