0000000000365423
AUTHOR
Duane R. Schultz
The second component of human complement: Use of glycosidases and glucosylation to distinguish the two forms
Abstract The two forms of human plasma C2 that were described in the preceding report (1) were investigated for their functional and biochemical differences. Incubation with the neuraminidase (NAN'dase) of Clostridium perfringens at 37°C resulted in a four- to fivefold increase in the hemolytic activity of both forms. The increase in activity was different than the increase caused by treatment with iodine. The mechanism of increased activity of NAN'dase-treated C2 was the generation of increased molecules of activated C3 (C3b), resulting in more molecules of C5 binding to (C4b, 2a, 3b)n. Removal of N-acetyl-neuraminate from C2 did not alter its binding to a cationic exchanger. Nonenzymatic …
The second component of human complement: Detection of two hemolytic forms in plasma by pH Variation
The second component of human complement (C2) in pseudoglobulin prepared from normal plasma eluted as a single peak at high conductivity (30 mS) and pH 4.5 from the cationic exchangers S-Sepharose or Mono S in the Fast Protein Liquid Chromatography (FPLC) System. The C2 was stable at pH 4.5 and 0 degrees C if enzyme inhibitors were used and the pH was raised to 6.0 after elution from the columns. After rechromatography on Mono S in the FPLC System at the median isoelectric point of 5.5 or pH 6.0, the C2 eluted as two distinct hemolytic forms: the first peaked at 16 mS, the second at 30 mS. The two forms of C2 did not correlate with the allotypic variant of C2 in individual, normal human pla…