Human complement component C3: characterization of active C3 S and C3 F, the two common genetic variants
Research output: Contribution to journal › Journal article › Research › peer-review
The two common genetic variants of human C3, C3 S and C3 F, were purified and characterized by SDS-PAGE, agarose gel electrophoresis, isoelectric focusing and amino acid analysis. The difference in electrophoretic mobility between the two variants was conserved after purification, and by isoelectric focusing of the hemolytically active proteins, pI values of 5.86 and 5.81 were determined for C3 S and C3 F, respectively. Any difference in amino acid composition was too small to be detected by amino acid analysis, and the two proteins had the same molecular weight as determined by SDS-PAGE.
| Original language | English |
|---|---|
| Journal | Molecular Immunology |
| Volume | 22 |
| Issue number | 8 |
| Pages (from-to) | 1005-8 |
| Number of pages | 4 |
| ISSN | 0161-5890 |
| Publication status | Published - Aug 1985 |
| Externally published | Yes |
- Amino Acids, Chemical Phenomena, Chemistry, Complement C3, Electrophoresis, Agar Gel, Electrophoresis, Polyacrylamide Gel, Genetic Variation, Humans, Isoelectric Focusing, Molecular Weight, Journal Article, Research Support, Non-U.S. Gov't
Research areas
ID: 180824490