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The Formation of Amyloid-Like Fibrils in Vitro from Bence Jones Proteins of the VI Subclass¹

From the Department of Medicine, New York University Medical Center School of Medicine, New York, New York 10016

Abstract

Sixty-one -Bence Jones proteins (BJP) including all known V subclasses were digested with pepsin. Forty-six formed a precipitate but only nine of these disclosed some of the characteristics of amyloid as revealed by congo red binding, green polarization birefringence, dichroism and fibrillar structures in the electron microscope. Eight of nine amyloid-forming BJP belonged to the VI subclass. Thirteen other BJP of the same subclass did not form amyloid under the conditions employed. The ability to form amyloid was unrelated to the constant region Oz marker.

Footnotes

¹ Presented in part at the Third Tagung der Gesellschaft für Immunologie, Marburg 1971. This work was supported by United States Public Health Service Grants AM-01431, AM-02594, and AM-012274; the Michael and Helen Schaffer Fund; and the New York Chapter of the Arthritis Foundation, Inc.

² Scholarship of the Deutscher Akademischer Austauschdienst, Bad Godesberg, Germany.

³ Medizinische Universitätsklinik, Tübingen, Germany.

⁴ Research Career Development Award, United States Public Health Service (5 KO3 AI 09572).

⁵ Career Scientist, The Health Research Council of the City of New York, I-274.

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