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Nephritic Factor: Its Structure and Function and Its Relationship to Initiating Factor of the Alternative Pathway
Author(s) -
SCHREIBER R. D.,
GÖTZE O.,
MÜLLEREBERHARD H. J.
Publication year - 1976
Publication title -
scandinavian journal of immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.934
H-Index - 88
eISSN - 1365-3083
pISSN - 0300-9475
DOI - 10.1111/j.1365-3083.1976.tb03020.x
Subject(s) - c3 convertase , chemistry , alternative complement pathway , enzyme , biochemistry , binding site , function (biology) , biophysics , microbiology and biotechnology , biology , immunology , antibody , complement system
Nephritic factor (NF) has a molecular weight of 170,000 and is composed of two disulfide‐linked 85,000‐dalton chains. NF assembles the fluid‐phase C3 convertase from Factors B and D, C3, and magnesium by physically incorporating itself into the enzyme complex. NF exerts its stabilizing effect on the cell‐bound C3/C5 convertase, EC, by physically associating itself with this complex. On decay of the cell‐bound enzyme NF is released into the fluid phase and retains its binding and stabilizing potential. Its activity is resistant to diisopropylfluorophosphate treatment. Because NF causes agglutination of EC, it must be endowed with more than one binding site.