(1) Guinea pig (Hartley strain) 内リンパ液中には, 補体が存在し, その補体価は3.70u/mlであった.(2) Guinea pig (Hartley strain) と C4D Guinea pig をウサギの血管条+Complete Adjuvant (Freund s') を抗原として, 感作すると Guinea pig (Hartley strain) 10匹中4匹に内リンパ水腫の発現があった. C4D Guinea pig 18 匹には内リンパ水腫が認められなかった.上記の結果より内リンパ液中に補体が存在し, 局所でのICの形成の可能性や感染防禦に重要な役割を演じ, また内リンパ水腫の発現には主に classical pathway が関与していると考える.

Endolymphatic hydrops

Strain (injury)

10.5631/jibirin.77.10special_2148

Cite

Citations (0)

Characterization of the arginine deiminase ofStreptococcus equisubsp.zooepidemicus

Canadian Journal of Microbiology (2006)

Kyongsu Hong

Streptococcus equi subsp. zooepidemicus is an important cause of infectious diseases in horses and rarely humans. Little is known about the virulence factors or protective antigens of S. equi subsp. zooepidemicus. In the present study, I designed original primers based on an alignment of the gene sagp(arcA) from Streptococcus pyogenes encoding streptococcal acid glycoprotein – arginine deiminase (SAGP/AD) to amplify the S. equi subsp. zooepidemicus counterpart sequence by polymerase chain reaction, and I analyzed the sagp(arcA) gene of the organism. Using chromosomal walking steps, I identified a contiguous eight-gene locus involved in SAGP/AD production. Their open reading frames were found to share significant homologies and to correspond closely in molecular mass to previously sequenced arc genes of S. pyogenes, thus they were designated ahrC.2 (arginine repressor), arcR (CRP/FNR transcription regulator), sagp(arcA) (streptococcal acid glycoprotein – arginine deiminase), putative acetyltransferase gene, arcB (ornithine carbamyl transferase), arcD (arginine–ornithine antiporter), arcT (Xaa-His peptidase), and arcC (carbamate kinase). The SAGP homologue of S. equi subsp. zooepidemicus (SzSAGP), encoded by arcA gene of the bacteria (arcA(SZ)), was successfully expressed in Escherichia coli and purified to homogeneity. When in vitro growth inhibitory activity of the recombinant SzSAGP was tested against MOLT-3 cells, it inhibited the growth of the cells during the 3 days of culture in a dose-dependent manner, accompanied by the induction of apoptotic cell death. The recombinant protein also possessed AD activity. By immunoblot analysis using both anti-SzSAGP-SfbI(H8) and anti-SfbI(H8) sera, I was able to demonstrate that the SzSAGP protein is expressed on the streptococcal surface.Key words: SAGP, arginine deiminase, Streptococcus equi subsp. zooepidemicus.

Arginine deiminase

Streptococcus equi

Streptococcus Pyogenes

10.1139/w06-041

Cite

Citations (5)

Eighth component of guinea pig complement. Purification and characterization

Molecular Immunology (1982)

Kozo Inoue Taroh Kinoshita Kyongsu Hong Kiyoshi Kondo

Lectin pathway

Properdin

C-type lectin

Complement control protein

Collectin

Ficolin

10.1016/0161-5890(82)90073-6

Cite

Citations (0)

Decreased Activity of Complement-Mediated Immune Complex Clearance in Hemodialysis Patients

Clinical Immunology and Immunopathology (1993)

Reiko Inagi Toshio Miyata Kyongsu Hong Patcharin Pramoonjago Kenji Maeda

Immune complex

Complement

Complement factor B

Immune adherence

10.1006/clin.1993.1135

Cite

Citations (6)

Characterization of Group A Streptococcal M23 Protein and Comparison of the M3 and M23 Protein’s Ligand-Binding Domains

Current Microbiology (2007)

Kyongsu Hong

Protein G

Protein A/G

10.1007/s00284-007-9012-9

Cite

Citations (8)

Rapid and simple measurement of human C5a-des-Arg level in plasma or serum using monoclonal antibodies

Journal of Immunological Methods (1987)

Junji Takeda Taroh Kinoshita Y. Takata Haruo Kozono Etsuko Tanaka

10.1016/0022-1759(87)90159-1

Cite

Citations (16)

Transport of Nattokinase across the Rat Intestinal Tract.

Biological and Pharmaceutical Bulletin (1995)

Mitsugu Fujita Kyongsu Hong Yae Ito S. Misawa Naoto Takeuchi

Intraduodenal administration of nattokinase (NK) at a dose of 80 mg/kg, resulted in the degradation of fibrinogen in plasma suggesting transport of NK across the intestinal tract in normal rats. The action of NK on the cleavage of fibrinogen in the plasma from blood samples drawn at intervals after intraduodenal administration of the enzyme was investigated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and Western blotting analysis with an anti-fibrinogen gamma chain antibody. The 270 kDa fragment carrying antigenic sites for the binding of the anti-fibrinogen gamma chain antibody appeared within 0.5 h and was then degraded gradually to a 105 kDa fragment via a 200 kDa fragment. This suggests that fibrinogen was degraded to a 105 kDa fragment via several intermediates (270 and 200 kDa). In parallel with the degradation process, plasma recalcification times were remarkably prolonged NK was also detected in the plasma from blood samples drawn 3 and 5 h after administration of the enzyme by SDS-PAGE and Western blotting analysis with an anti-NK antibody. The results indicate that NK is absorbed from the rat intestinal tract and that NK cleaves fibrinogen in plasma after intraduodenal administration of the enzyme.

Nattokinase

10.1248/bpb.18.1194

Cite

Citations (101)

EPITOPE ANALYSIS OF STREPTOCOCCAL M3 ANTIGEN‐SPECIFIC MONOCLONAL ANTIBODY

Journal of Rapid Methods & Automation in Microbiology (2008)

Kyongsu Hong

ABSTRACT The binding domains of four monoclonal antibodies (mAbs) (4E10, 2C11, 1E10 and 3H9) specific for M3, the major protein surface antigen of Streptococcus pyogenes, were determined by Western blot analysis using truncated M3 polypeptides. The data indicate that epitopes for four mAbs are located within the B repeat block in M3 protein. A sandwich enzyme‐linked immunosorbent assay for detecting of M3 protein was established using these mAbs and polyclonal anti‐M3 antibody. The technique would be beneficial to our understanding of the epidemiology and to better control of streptococcal diseases. PRACTICAL APPLICATIONS Severe invasive diseases such as streptococcal toxic shock‐syndrome and necrotizing fasciitis have been mainly caused by M1 and M3 serotypes. The M types are also associated with acute rheumatic fever (ARF). Importantly, serotype M3 strains cause a higher rate of lethal infections than other group A streptococcus (GAS) M types. Since epitopes for four monoclonal antibodies (mAbs) are located within the B repeat block in M3 protein, assays for detecting of the epitopes using the mAbs could be helpful for the detection of severe invasive diseases or ARF.

Streptococcus Pyogenes

Polyclonal antibodies

10.1111/j.1745-4581.2008.00118.x

Cite

Citations (0)

Effect of trypsinization on the activity of human β 1H globulin

Molecular Immunology (1982)

Inoue Kozo Kyongsu Hong Taroh Kinoshita

Trypsinization

Atmospheric temperature range

Emission intensity

Nanosensor

10.1016/0161-5890(82)90072-4

Cite

Citations (0)