Faculty Profiles - SAWA Yoshihiko

MISC - SAWA Yoshihiko

Division display 261 - 270 of about 270 ／ All the affair displays >>

Mycoplasma salivarium(MS)のヒトIgG Fc結合活性について

沢禎彦

北海道歯学雑誌 15 ( 2 ) 276 - 290 1994.12

Language：Japanese Publisher：北海道歯学会

MS細胞は,ヒトIgG Fc断片と結合した。結合活性はpH 7.0よりもpH 4.0で強く,Mn2+ならびにCu2+で増強されたが,マンノースで阻害された。MS細胞のプロナーゼ処理によって,IgG Fc断片結合活性が著しく低下し,分子量150, 90ならびに88kDaのタンパク質が減少または消失した。MS細胞はレクチン様活性で,マンノース特異的にIgG Fc部位の糖鎖と結合し,結合に関与するのは分子量が150, 90ならびに88kDaの細胞表層タンパク質である。IgG Fc断片と結合する主要タンパク質は,分子量90kDaのタンパク質(90kp)であることがイムノブロッティング法で証明された

researchmap

MEMBRANE-PROTEINS WITH MOLECULAR MASSES OF 88-KDA, 90-KDA AND 150-KDA ARE RESPONSIBLE FOR BINDING OF HUMAN-IMMUNOGLOBULIN-G FC-FRAGMENT TO THE NATIVE CELLS OF MYCOPLASMA-SALIVARIUM

K SHIBATA, Y SAWA, S INOUE, M NODA, T WATANABE

FEMS MICROBIOLOGY LETTERS 123 ( 3 ) 305 - 309 1994.11

Language：English Publisher：ELSEVIER SCIENCE BV

Mycoplasma salivarium cells bound the Fc fragment of human immunoglobulin G. The activity was remarkably enhanced by Mn2+, but not by Mg2+ and Ca2+; significantly inhibited by D-mannose; and reduced by pronase treatment of the cells. About 90% of the cells treated with pronase were not disrupted. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of proteins of the cells treated with pronase indicated that proteins with molecular masses of 88, 90 and 150 kDa (88 kp, 90 kp and 150 kp) were specifically digested. The results presented suggest that 88 kp, 90 kp and 150 kp, located in the outer surface of the cell membrane, are responsible for the activity of the M. salivarium cells and interact with a carbohydrate-containing moiety (D-mannose) of the Fc fragment in a Mn2+-dependent manner.

DOI： 10.1016/0378-1097(94)90209-7

Mycoplasma salivarium細胞のヒトIgG Fc結合活性について

沢禎彦

歯科基礎医学会雑誌 36 ( 抄録 ) 93 - 93 1994.9

Mycoplasma salivarium細胞のヒトIgG Fc結合活性について

沢禎彦

日本細菌学雑誌 49 ( 2 ) 436 - 436 1994.3

ACID-PHOSPHATASE PURIFIED FROM MYCOPLASMA-FERMENTANS HAS PROTEIN-TYROSINE PHOSPHATASE-LIKE ACTIVITY

KI SHIBATA, M NODA, Y SAWA, T WATANABE

INFECTION AND IMMUNITY 62 ( 1 ) 313 - 315 1994.1

Language：English Publishing type：Article, review, commentary, editorial, etc. (scientific journal) Publisher：AMER SOC MICROBIOLOGY

Acid phosphatase purified from Mycoplasma fermentans dephosphorylated phosphotyrosine-containing lysozyme and Raytide, a peptide substrate for protein tyrosine phosphatases. The optimum pH for Raytide was about 5.5. Raytide phosphatase activity was inhibited by potassium fluoride, sodium molybdate, and sodium orthovanadate and was found to exist in some mycoplasmas.

Web of Science

researchmap

PURIFICATION AND CHARACTERIZATION OF MEMBRANE-PROTEIN (90 KDA) FROM MYCOPLASMA SALIVARIUM, WHICH BINDS IMMUNOGLOBULIN (IG)G FC FRAGMENT

Y SAWA, K SHIBATA, M NODA, T WATANABE

MICROBIOLOGY AND IMMUNOLOGY 38 ( 4 ) 257 - 262 1994

Language：English Publisher：CENTER ACADEMIC PUBL JAPAN

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.

Web of Science

researchmap

Purification and Characterization of an Acid Phosphates from ┣DBMycoplasma fragments(/)-┫DB(共著)

Microbiology and Immunology 38 ( 2 ) 103 - 107 1994

Human immunoglobulin G Fc binding activity of Mycoplasma salivarium.

沢禎彦

北海道歯学雑誌 15 ( 2 ) 1994

ヒトIgGのFc部位と結合するMycoplasma salivariumの細胞膜タンパク質について

沢禎彦

歯科基礎医学会雑誌 35 ( 抄録 ) 185 - 185 1993.9

Immunoglobulin G Fc Fragment‐Binding Proteins in Mycoplasma salivarium Cells

Yoshihiko Sawa, Tsuguo Watanabe, Ken‐ichiro Shibata

Microbiology and Immunology 36 ( 6 ) 655 - 659 1992

Language：English

Cell proteins of Mycoplasma salivarium were separated by sodium dodecyl sulfate‐polyacrylamide gel electrophoresis, transferred to membranes, then examined for reactivity with human IgG molecules, the Fc fragment of human IgG, and concanavalin A (ConA). Multiple protein bands bound IgG, and most of them also bound ConA. One (corresponding to a molecular mass of 90 kDa) of the IgG‐ and ConA‐binding bands intensely interacted with the Fc fragment of IgG. The reactivity of proteins eluted from the band with the Fc fragment, tested by dot‐blotting and ELISA, was inhibited (90%) by pre‐incubation with IgG and to a lesser extent (50%), with IgM. Thus, M. salivarium contained a cellular protein with a molecular mass of 90 kDa, that bound the Fc fragment of human IgG. © owned by Center for Academic Publications Japan (Publisher)

DOI： 10.1111/j.1348-0421.1992.tb02067.x

Scopus

PubMed

researchmap

　 PREV - NEXT 　

< SAWA Yoshihiko >

MISC - SAWA Yoshihiko