Date of Award
1998
Document Type
Thesis
Publication Status
Version of Record
Submission Date
October 2026
Thesis/Dissertation Advisor [Chair]
Hartmann, James X.
Abstract
This study describes an affinity method which purifies albumin from fish serum. Hybridoma clones producing antibodies specific to fish albumin have been screened and propagated and their antibodies coupled to a cross-linked agarose gel matrix which has been activated with N-hydroxysuccinimide. The resulting gel with its ligand attached was then used to purify albumin from fish serum. The procedure was optimized for coupling, sample application and elution. The coupling optimization using varying pH values resulted in over 90% coupling efficiencies. The sample application optimization showed yields of 2 mg of protein per ml of serum at 1:5 dilution of sample. Elution conditions were evaluated using varying pH and chaotropic agent concentrations. The optimal elution conditions (pH 4.0) resulted in a yield of 0.2 mg/ml of gel with several impurities. Elution at pH 3.0 resulted in a very pure product with low yield (.02 mg/ml of gel) and a loss of activity.
Extent
51 p.
Recommended Citation
Apter, Christine V., "Immunoaffinity purification of albumin from fish serum" (1998). Electronic Theses and Dissertations 1990 - 1999. 1317.
https://digitalcommons.fau.edu/etd_general_4/1317
Identifier
FADT15568
Comments
Charles E. Schmidt College of Science|Thesis (M.S.)--Florida Atlantic University, 1998.|FAU Electronic Theses and Dissertations Collection|Charles E. Schmidt College of Science