Biosynthesis of pro-C3, a precursor of the third component of complement.
V Brade, RE Hall, HR Colten - The Journal of experimental medicine, 1977 - rupress.org
V Brade, RE Hall, HR Colten
The Journal of experimental medicine, 1977•rupress.orgA precusor of the third component of complement, pro-C3, was detected in studies of cell-
free synthesis and intracellularly in homogenates of liver tissue cultures. The molecular
weight of pro-C3 was indistinguishable from that of intact native C3 secreted in vitro by liver
or peritoneal macrophages, but its structure was different. Pro-C3 is a single polypeptide
chain, whereas C3 secreted by cells in culture consists of two polypeptide chains (mol wt
120,000 and 76,000) linked by disulfide bonds.
free synthesis and intracellularly in homogenates of liver tissue cultures. The molecular
weight of pro-C3 was indistinguishable from that of intact native C3 secreted in vitro by liver
or peritoneal macrophages, but its structure was different. Pro-C3 is a single polypeptide
chain, whereas C3 secreted by cells in culture consists of two polypeptide chains (mol wt
120,000 and 76,000) linked by disulfide bonds.
A precusor of the third component of complement, pro-C3, was detected in studies of cell-free synthesis and intracellularly in homogenates of liver tissue cultures. The molecular weight of pro-C3 was indistinguishable from that of intact native C3 secreted in vitro by liver or peritoneal macrophages, but its structure was different. Pro-C3 is a single polypeptide chain, whereas C3 secreted by cells in culture consists of two polypeptide chains (mol wt 120,000 and 76,000) linked by disulfide bonds.
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