Biomaterial Database

Separation of functionally or highly pure C2 from human plasma with Sepharose and a lectin of Euonymus europeus. 1984

D R Schultz, and P I Arnold

A method is described for isolating both functionally and highly pure C2 from normal human serum or plasma. Functionally pure C2 was obtained by a two-step method of ammonium sulfate (AS) fractionation of plasma or serum and chromatography on AH-Sepharose containing a bound lectin of Euonymus europeus. The functionally pure C2 can be isolated in 2 days, and is used routinely as a reagent for functional hemolytic titrations of C3 and C4 in the Clinical Immunology Laboratory. Highly pure C2 was isolated by the two-step fractionation with AS followed by chromatography on CM-cellulose, aged CNBr-activated Sepharose 4B, and AH-Sepharose-lectin. The major difficulty for isolating highly pure C2 was its separation from Factor B of the alternative complement pathway. The yield of C2 varied from 30 to 40 per cent. Following electrophoresis and staining on polyacrylamide gels, the single band was hemolytically active C2.

UI	MeSH Term	Description	Entries
D011415	Complement Factor B	A glycine-rich, heat-labile serum glycoprotein that contains a component of the C3 CONVERTASE ALTERNATE PATHWAY (C3bBb). Bb, a serine protease, is generated when factor B is cleaved by COMPLEMENT FACTOR D into Ba and Bb.	C3 Proactivator,C3PA,Complement 3 Proactivator,Factor B,Properdin Factor B,Bb Fragment of Factor B,Complement Factor B Fragment, Bb,Complement Factor B, Alternative Pathway,Complement Factor B-Derived Fragment Bb,Complement Factor Ba,Complement Factor Bb,Complement Protein B,Complement Protein Factor B,Properdin Factor Ba,Properdin Factor Bb,Properdin Factor Bf,Properdin Factor Bf F1,Bb, Complement Factor,Complement Factor B Derived Fragment Bb,Factor B, Complement,Factor B, Properdin,Factor Ba, Complement,Factor Ba, Properdin,Factor Bb, Complement,Factor Bb, Properdin,Factor Bf, Properdin,Proactivator, C3,Proactivator, Complement 3,Protein B, Complement
D002847	Chromatography, Agarose	A method of gel filtration chromatography using agarose, the non-ionic component of agar, for the separation of compounds with molecular weights up to several million.	Chromatography, Sepharose,Agarose Chromatography,Sepharose Chromatography,Agarose Chromatographies,Chromatographies, Agarose,Chromatographies, Sepharose,Sepharose Chromatographies
D003175	Complement C2	A component of the CLASSICAL COMPLEMENT PATHWAY. C2 is cleaved by activated COMPLEMENT C1S into COMPLEMENT C2B and COMPLEMENT C2A. C2a, the COOH-terminal fragment containing a SERINE PROTEASE, combines with COMPLEMENT C4B to form C4b2a (CLASSICAL PATHWAY C3 CONVERTASE) and subsequent C4b2a3b (CLASSICAL PATHWAY C5 CONVERTASE).	C2 Complement,Complement 2,Complement Component 2,C2, Complement,Complement, C2,Component 2, Complement
D006801	Humans	Members of the species Homo sapiens.	Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D037102	Lectins	Proteins that share the common characteristic of binding to carbohydrates. Some ANTIBODIES and carbohydrate-metabolizing proteins (ENZYMES) also bind to carbohydrates, however they are not considered lectins. PLANT LECTINS are carbohydrate-binding proteins that have been primarily identified by their hemagglutinating activity (HEMAGGLUTININS). However, a variety of lectins occur in animal species where they serve diverse array of functions through specific carbohydrate recognition.	Animal Lectin,Animal Lectins,Isolectins,Lectin,Isolectin,Lectin, Animal,Lectins, Animal