Abstract
Proteins which were able to bind noncovalently with mouse factor B were found in cells that are nonsecretors of factor B such as mouse‐established monocytic cells and L cells but not in peritoneal resident macrophages. These proteins were isolated from lysates of L cells and separated into four distinct proteins by preparative SDS‐polyacrylamide gel electrophoresis, with molecular weights of 25K, 28K, 33K, and 35K. The individual proteins formed a complex with purified mouse factor B at a molecular ratio of 1: 1 and inhibited its hemolytic activity. Proteins 25K and 28K inhibited the hemolytic activity of an activated form of factor B combined with cobra venom factor as well as that of the native form. These inhibitors did not affect the hemolytic activity of the second component of complement in mouse serum. The inhibitory activity of the 25K protein was partially inhibited by antiserum raised against it in rabbits.
| Original language | English |
|---|---|
| Pages (from-to) | 1079-1091 |
| Number of pages | 13 |
| Journal | Microbiology and Immunology |
| Volume | 27 |
| Issue number | 12 |
| DOIs | |
| Publication status | Published - 1983 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Microbiology
- Immunology
- Virology
Cite this
Endogenous Inhibitors of Factor B. / Moriyama, Takeshi; Kawamoto, Yasuko; Ichikawa, Hidetaka; Okamoto, Keinosuke; Inoue, Takashi; Kobayashi, Tatsuhiko; Miyama, Akio.
In: Microbiology and Immunology, Vol. 27, No. 12, 1983, p. 1079-1091.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Endogenous Inhibitors of Factor B
AU - Moriyama, Takeshi
AU - Kawamoto, Yasuko
AU - Ichikawa, Hidetaka
AU - Okamoto, Keinosuke
AU - Inoue, Takashi
AU - Kobayashi, Tatsuhiko
AU - Miyama, Akio
PY - 1983
Y1 - 1983
N2 - Proteins which were able to bind noncovalently with mouse factor B were found in cells that are nonsecretors of factor B such as mouse‐established monocytic cells and L cells but not in peritoneal resident macrophages. These proteins were isolated from lysates of L cells and separated into four distinct proteins by preparative SDS‐polyacrylamide gel electrophoresis, with molecular weights of 25K, 28K, 33K, and 35K. The individual proteins formed a complex with purified mouse factor B at a molecular ratio of 1: 1 and inhibited its hemolytic activity. Proteins 25K and 28K inhibited the hemolytic activity of an activated form of factor B combined with cobra venom factor as well as that of the native form. These inhibitors did not affect the hemolytic activity of the second component of complement in mouse serum. The inhibitory activity of the 25K protein was partially inhibited by antiserum raised against it in rabbits.
AB - Proteins which were able to bind noncovalently with mouse factor B were found in cells that are nonsecretors of factor B such as mouse‐established monocytic cells and L cells but not in peritoneal resident macrophages. These proteins were isolated from lysates of L cells and separated into four distinct proteins by preparative SDS‐polyacrylamide gel electrophoresis, with molecular weights of 25K, 28K, 33K, and 35K. The individual proteins formed a complex with purified mouse factor B at a molecular ratio of 1: 1 and inhibited its hemolytic activity. Proteins 25K and 28K inhibited the hemolytic activity of an activated form of factor B combined with cobra venom factor as well as that of the native form. These inhibitors did not affect the hemolytic activity of the second component of complement in mouse serum. The inhibitory activity of the 25K protein was partially inhibited by antiserum raised against it in rabbits.
UR - http://www.scopus.com/inward/record.url?scp=0021076794&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0021076794&partnerID=8YFLogxK
U2 - 10.1111/j.1348-0421.1983.tb02941.x
DO - 10.1111/j.1348-0421.1983.tb02941.x
M3 - Article
C2 - 6374390
AN - SCOPUS:0021076794
VL - 27
SP - 1079
EP - 1091
JO - Microbiology and Immunology
JF - Microbiology and Immunology
SN - 0385-5600
IS - 12
ER -