Biosynthesis of the internal thioester bond of the third component of complement.

Abstract:

:C3-translational product, which was synthesized with rabbit liver mRNA in a reticulocyte lysate protein-synthesizing system, did not react with [14C]methylamine, indicating the lack of an internal thioester bond. Instead, the C3-translational product reacted with iodo[1-14C]acetamide, as determined by gel electrophoresis in the presence of sodium dodecyl sulfate after immunoprecipitation of the product, indicating the presence of a reactive thiol group. When the C3-translational product was treated with rabbit liver homogenate, the product acquired reactivity with [14C]methylamine and lost the reactivity with iodo[1-14C]acetamide. Thus, the liver homogenate seemed to contain a factor (or factors) required for the formation of an internal thioester bond. The factor was partially purified from the liver homogenate by ammonium sulfate precipitation and ion-exchange chromatography on DEAE-cellulose.

journal_name

J Biochem

journal_title

Journal of biochemistry

authors

Iijima M,Tobe T,Sakamoto T,Tomita M

doi

10.1093/oxfordjournals.jbchem.a134983

subject

Has Abstract

pub_date

1984-11-01 00:00:00

pages

1539-46

issue

5

eissn

0021-924X

issn

1756-2651

journal_volume

96

pub_type

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