Analysis of Major Surface Polypeptides of Rickettsia japonica

Takahiro Uchida; David H. Walker; Tsuneo Uchiyama

doi:10.1111/j.1348-0421.1994.tb01825.x

Analysis of Major Surface Polypeptides of Rickettsia japonica

Takahiro Uchida, David H. Walker, Tsuneo Uchiyama

Pathology

Research output: Contribution to journal › Article › peer-review

9 Scopus citations

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
DOIs	https://doi.org/10.1111/j.1348-0421.1994.tb01825.x
State	Published - 1994

Keywords

Peptide mapping
Rickettsia japonica
Spotted fever group rickettsiae
Surface polypeptides

ASJC Scopus subject areas

Microbiology
Immunology
Virology

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10.1111/j.1348-0421.1994.tb01825.x

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title = "Analysis of Major Surface Polypeptides of Rickettsia japonica",

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.",

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AU - Uchida, Takahiro

AU - Walker, David H.

AU - Uchiyama, Tsuneo

PY - 1994

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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

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