European Journal of Immunology · 1989 · 65 citations · 17 references
Life SciencesBiochemistryMolecular BiologyClinical BiochemistryGene ExpressionMolecular ImmunologyComplement SystemPlasma ProteinsC3 CleavageComplement ComponentsComplement Protein ProcessingImmunoaffinity Purification
In addition to the 150-kDa factor H protein, we have previously described a 43-kDa factor H molecule in human plasma, which probably represents a translational product of the additional 1.8-kb mRNA for factor H. This factor H was isolated from human plasma by means of immunoaffinity chromatography and high-performance liquid chromatography. When tested for its functional activity, this purified 43-kDa H protein was shown to act as cofactor for factor I- mediated cleavage of fluid-phase C3b to iC3b.
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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
Ulrich K. Laemmli · Nature · 1970 · 251.6K citations
Michael K. Pangburn, Robert D. Schreiber, Hans J. Müller‐Eberhard · The Journal of Experimental Medicine · 1977 · 684 citations · Full text