The Journal of Experimental Medicine, Vol 128, 571-593,
Copyright © 1968 by The Rockefeller University Press
THE ENZYMATIC NATURE OF C'1r
:
CONVERSION OF C'1s TO C'1 ESTERASE AND DIGESTION OF AMINO ACID ESTERS BY C'1r
George B. Naff M.D.1 and
Oscar D. Ratnoff M.D.1
1 From the Department of Medicine, Case Western Reserve University School of Medicine, and University Hospitals, Cleveland, Ohio 44106
Human C'1, a macromolecular complex composed of three subunits, is the zymogen for at least two distinct enzymes. Preparations of one subunit, C'1r, functioned as a protease which converted another subunit, C'1s, to C'1 esterase. The conversion of C'1s to C'1 esterase by C'1r was blocked by Liquoid, phenyl methylsulfonyl fluoride, and calcium ions, but not by soybean trypsin inhibitor, hirudin, or heparin.
Preparations of C'1r also possessed two additional functions, i.e., the ability to hydrolyze certain synthetic amino acid esters and to participate in immune hemolysis. Evidence was presented which indicates that these three functions are properties of a single entity, C'1r, but not of the same portion of its molecular structure. These observations suggest that C'1r has at least two active sites, one for its reaction with C'1q, an additional subunit of C'1, and one for its reaction with C'1s; together, the three subcomponents, C'1q, C'1r, and C'1s, form a single functional unit, the first component of complement.
Submitted on March 31, 1968
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