| Range |
Table - link
|
| Organism |
Human Homo sapiens |
| Reference |
Vogel CW, Müller-Eberhard HJ. The cobra venom factor-dependent C3 convertase of human complement. A kinetic and thermodynamic analysis of a protease acting on its natural high molecular weight substrate. J Biol Chem. 1982 Jul 25 257(14):8292-9 p.8295 table IPubMed ID6919543
|
| Method |
Abstract: "Enzymes of the complement system exhibit, unlike most other proteases, a high substrate specificity, hydrolyzing only a single peptide bond in their protein substrates. This property allowed the performance of a detailed analysis of the enzymatic activity of a protease acting on its natural high molecular weight substrate." |
| Comments |
P.8295 left column 3rd paragraph: "Table I lists the kinetic parameters determined for each of the four temperatures. Mean values and standard deviations have been calculated for the parameters Km, turnover number, and ko =v/[S] which were determined by several individual experiments. The other parameters were derived from these mean values. Since the CVF-dependent C3 convertase has only one catalytic subunit/molecule, the turnover number is identical with the catalytic center activity. Up to a C3 concentration of about 3×10^-6M, the substrate turnover can be described as a first order reaction. The apparent first order rate constants, ko, were determined by two methods as described under “Experimental Procedures” and are also listed in Table I." |
| Entered by |
Uri M |
| ID |
114395 |