Studies On The Second Complement Component (c2n) Of The Nurse Shark (ginglymostoma Cirratum)
Date of Award
Doctor of Philosophy (Ph.D.)
C2n was isolated and purified from nurse shark serum by initial cold low ionic strength precipitation, followed by ion exchange chromatography on DE-52 cellulose, adsorbtion/desorbtion on hydroxylapatite and filtration on Bio-Gel A-0.5. The final purification step used was polyacrylamide disc gel electrophoresis. The molecular weight of C2n was determined by gel filtration on Bio-Gel A-0.5 and Sephacryl S-200, and polyacrylamide disc gel electrophoresis: values obtained were 1.7 x 10('5) daltons, 1.6 x 10('5) daltons and 1.8 x 10('5) daltons respectively. C2n is heat stable, retaining 100% activity after heating for 2 hours at 56(DEGREES)C. The component is not compatible with guinea pig C2 and interfers with the lysis of EAnC1n by guinea pig C4 in the presence of C4-deficient serum. No appreciable decay of EAnC1nC2n was noted in 1 hour at 30(DEGREES)C. Comparative studies suggest C2n to be analogous to its mammalian counterpart, C4.
Smith, Sylvia Hyder, "Studies On The Second Complement Component (c2n) Of The Nurse Shark (ginglymostoma Cirratum)" (1983). Dissertations from ProQuest. 1343.