Characterization of Clq, Cls and Cl̄ Inh synthesized by stimulated human monocytes in vitro
- 7 October 1985
- journal article
- Published by Wiley in FEBS Letters
- Vol. 190 (1), 65-68
- https://doi.org/10.1016/0014-5793(85)80428-2
Abstract
Clq, Cls and Cl̄ Inh synthesized and secreted by human monocytes were characterized by SDS‐PAGE. Clq is formed of three chains A (M r ~35000), B (M r ~33000) and C (M r ~25000) which are associated in two subunits A‐B and C‐C. It appears identical to C1q purified from plasma. Cls is secreted as a non‐activated, monocatenar protein of M r ~87000 identical to proenzymic Cls from plasma. Secreted Cl̄ Inh (M r ~100000) has a slightly higher M r than purified plasmatic Cl̄ Inh. Monensin treatment of the cells favours the intracytoplasmic accumulation of products at various glycosylation stages.This publication has 11 references indexed in Scilit:
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