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J Virol. 1971 May; 7(5): 569-576
Copyright © 1971 American Society for Microbiology. All Rights Reserved.

Australia Antigen: Large-Scale Purification from Human Serum and Biochemical Studies of Its Proteins

^a Rockville Laboratory ^,1 of the Molecular Anatomy Program, Oak Ridge National Laboratory, ^,2 Rockville, Maryland 20852
^b Laboratory of Infectious Diseases, National Institute of Allergy and Infectious Diseases, Bethesda, Maryland 20014
^c Blood Bank Department, Clinical Center, National Institutes of Health, Bethesda, Maryland 20014

ABSTRACT

Biophysical techniques are described for the large-scale isolation of Australia antigen (Au) from unit quantities of human serum by using the batch-type zonal centrifuge rotors. A three-step procedure involving isopycnic banding of the particle in CsCl density gradients and rate-zonal centrifugation on sucrose gradients resulted in a highly purified Au preparation which was used for biochemical studies of Au proteins and as immunizing antigen for the production of reagent antiserum in animals. The spherical form of Au, which was devoid of detectable nucleic acid, was composed of two major proteins (AuP1 and AuP2) and a minor protein (AuP3) of 26,000, 32,000, and 40,000 molecular weight, respectively, as determined by acrylamide gel electrophoresis. The significance of these findings to the possibility of Au subtypes is discussed.

¹ The Rockville Laboratory of the Molecular Anatomy Program is supported by a collaborative program between the Division of Biology and Medicine, U.S. Atomic Energy Commission, and the National Institute of Allergy and Infectious Diseases.

² Operated by Union Carbide Corporation Nuclear Division for the U.S. Atomic Energy Commission.

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