Purification and Characterization of Membrane Protein (90 kDa) from Mycoplasma salivarium, Which Binds Immunoglobulin (Ig) G Fc Fragment

Yoshihiko Sawa; Ken Ichiro Shibata; Mamoru Noda; Tsuguo Watanabe

doi:10.1111/j.1348-0421.1994.tb01773.x

Purification and Characterization of Membrane Protein (90 kDa) from Mycoplasma salivarium, Which Binds Immunoglobulin (Ig) G Fc Fragment

Yoshihiko Sawa, Ken Ichiro Shibata, Mamoru Noda, Tsuguo Watanabe

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

3 Citations (Scopus)

Abstract

A 90 kDa protein of Mycoplasma salivarium was released from cell membranes of the organism with Triton X-100 and purified by ion-exchange chromatography and chromatofocusing. The protein was eluted at pH 5.5 by chromatofocusing. The protein was shown to react with the Fc fragments of IgG from human and nine different animal species and did not distinguish between IgG from different species, while protein A, tested for comparative purposes, displayed a strong specificity for human and swine IgG. Furthermore, the protein reacted with antigen specific goat IgG (specific for gamma chains of human IgG), sheep red blood cells (SRBC) sensitized with rabbit antiserum to SRBC, that is, the Fc part of rabbit IgG, and concanavalin A as well. These findings may suggest that the protein is a lectin which binds the carbohydrate moiety of the Fc part of IgG.

Original language	English
Pages (from-to)	257-262
Number of pages	6
Journal	MICROBIOLOGY and IMMUNOLOGY
Volume	38
Issue number	4
DOIs	https://doi.org/10.1111/j.1348-0421.1994.tb01773.x
Publication status	Published - 1994
Externally published	Yes

Keywords

IgG Fc-binding protein
Mycoplasma salivarium

ASJC Scopus subject areas

Microbiology
Immunology
Virology

Access to Document

10.1111/j.1348-0421.1994.tb01773.x

Fingerprint Dive into the research topics of 'Purification and Characterization of Membrane Protein (90 kDa) from Mycoplasma salivarium, Which Binds Immunoglobulin (Ig) G Fc Fragment'. Together they form a unique fingerprint.

Cite this

@article{feb8ebe1be22430f98978e741914f221,

title = "Purification and Characterization of Membrane Protein (90 kDa) from Mycoplasma salivarium, Which Binds Immunoglobulin (Ig) G Fc Fragment",

abstract = "A 90 kDa protein of Mycoplasma salivarium was released from cell membranes of the organism with Triton X-100 and purified by ion-exchange chromatography and chromatofocusing. The protein was eluted at pH 5.5 by chromatofocusing. The protein was shown to react with the Fc fragments of IgG from human and nine different animal species and did not distinguish between IgG from different species, while protein A, tested for comparative purposes, displayed a strong specificity for human and swine IgG. Furthermore, the protein reacted with antigen specific goat IgG (specific for gamma chains of human IgG), sheep red blood cells (SRBC) sensitized with rabbit antiserum to SRBC, that is, the Fc part of rabbit IgG, and concanavalin A as well. These findings may suggest that the protein is a lectin which binds the carbohydrate moiety of the Fc part of IgG.",

keywords = "IgG Fc-binding protein, Mycoplasma salivarium",

author = "Yoshihiko Sawa and Shibata, {Ken Ichiro} and Mamoru Noda and Tsuguo Watanabe",

year = "1994",

doi = "10.1111/j.1348-0421.1994.tb01773.x",

language = "English",

volume = "38",

pages = "257--262",

journal = "Microbiology and Immunology",

issn = "0385-5600",

publisher = "Center for Academic Publications Japan",

number = "4",

}

TY - JOUR

T1 - Purification and Characterization of Membrane Protein (90 kDa) from Mycoplasma salivarium, Which Binds Immunoglobulin (Ig) G Fc Fragment

AU - Sawa, Yoshihiko

AU - Shibata, Ken Ichiro

AU - Noda, Mamoru

AU - Watanabe, Tsuguo

PY - 1994

Y1 - 1994

N2 - A 90 kDa protein of Mycoplasma salivarium was released from cell membranes of the organism with Triton X-100 and purified by ion-exchange chromatography and chromatofocusing. The protein was eluted at pH 5.5 by chromatofocusing. The protein was shown to react with the Fc fragments of IgG from human and nine different animal species and did not distinguish between IgG from different species, while protein A, tested for comparative purposes, displayed a strong specificity for human and swine IgG. Furthermore, the protein reacted with antigen specific goat IgG (specific for gamma chains of human IgG), sheep red blood cells (SRBC) sensitized with rabbit antiserum to SRBC, that is, the Fc part of rabbit IgG, and concanavalin A as well. These findings may suggest that the protein is a lectin which binds the carbohydrate moiety of the Fc part of IgG.

AB - A 90 kDa protein of Mycoplasma salivarium was released from cell membranes of the organism with Triton X-100 and purified by ion-exchange chromatography and chromatofocusing. The protein was eluted at pH 5.5 by chromatofocusing. The protein was shown to react with the Fc fragments of IgG from human and nine different animal species and did not distinguish between IgG from different species, while protein A, tested for comparative purposes, displayed a strong specificity for human and swine IgG. Furthermore, the protein reacted with antigen specific goat IgG (specific for gamma chains of human IgG), sheep red blood cells (SRBC) sensitized with rabbit antiserum to SRBC, that is, the Fc part of rabbit IgG, and concanavalin A as well. These findings may suggest that the protein is a lectin which binds the carbohydrate moiety of the Fc part of IgG.

KW - IgG Fc-binding protein

KW - Mycoplasma salivarium

UR - http://www.scopus.com/inward/record.url?scp=0028281350&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0028281350&partnerID=8YFLogxK

U2 - 10.1111/j.1348-0421.1994.tb01773.x

DO - 10.1111/j.1348-0421.1994.tb01773.x

M3 - Article

C2 - 7523837

AN - SCOPUS:0028281350

VL - 38

SP - 257

EP - 262

JO - Microbiology and Immunology

JF - Microbiology and Immunology

SN - 0385-5600

IS - 4

ER -