TY - JOUR
T1 - Human complement component C3
T2 - characterization of active C3 S and C3 F, the two common genetic variants
AU - Behrendt, N
PY - 1985/8
Y1 - 1985/8
N2 - 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.
AB - 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.
KW - Amino Acids
KW - Chemical Phenomena
KW - Chemistry
KW - Complement C3
KW - Electrophoresis, Agar Gel
KW - Electrophoresis, Polyacrylamide Gel
KW - Genetic Variation
KW - Humans
KW - Isoelectric Focusing
KW - Molecular Weight
KW - Journal Article
KW - Research Support, Non-U.S. Gov't
M3 - Journal article
C2 - 4047041
SN - 0161-5890
VL - 22
SP - 1005
EP - 1008
JO - Molecular Immunology
JF - Molecular Immunology
IS - 8
ER -