Purification and characterization of subcomponent C1q of the first component of bovine complement.
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Bovine complement subcomponent Clq was purified, in a highly hemolytically active form, by a combination of precipitation with EGTA, ion-exchange chromatography, and gel filtration. Yield ranged from 22 to 28% as protein amounts, and the activity of final preparations was in the range of 2×1013-4×1013 effective molecules/mg. The molecular weight of undissociated Clq was 407, 000, as determined by polyacrylamide gel electrophoresis containing sodium dodecyl sulfate (SDS). Clq was shown to be composed of two non-covalently linked subunits of approximately 46, 000 and 45, 000 molecular weights in a molar ratio of 2:1. On reduction, the higher molecular weight subunit gave two chains having approximate molecular weights of 23, 600 and 22, 200 in equimolar ratio, and the lower molecular weight subunit gave one chain with a molecular weight of approximately 22, 000. Clq contained hydroxyproline, hydroxylysine, a high percentage of glycine and approximately 9% carbohydrate and 14.8% nitrogen. The absorption coefficient (A1%1cm) in 300mM NaCl was found to be 7.3±0.12 at 280nm. From these results, overall molecular structure of bovine Clq looks similar to that of human complement subcomponent Clq.
- 社団法人 日本生化学会の論文
社団法人 日本生化学会 | 論文
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