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Fibrillar Assemblage of Variable Segments of Immunoglobulin Light Chains: An Electron Microscopic Study¹

From the Arthritis and Connective Tissue Disease Section of the Evans Department of Clinical Research, University Hospital, the Boston University Medical Services, Boston City Hospital, and the Department of Medicine, Boston University School of Medicine, Boston University Medical Center, Boston, Massachusetts 02118, and the Research Unit, JEOL (U.S.A.), Inc., Medford, Massachusetts 02155

Abstract

Bence Jones protein was enzymatically cleaved into its variable and constant segments, and then the variable segment was precipitated at neutral pH. The precipitate stained well with Congo red and showed green birefringence under the polarized light after such staining. High resolution electron microscopy of shadow-casted and negatively stained preparations revealed that they consisted of three types of fibrillar structures, respectively measuring 10 to 20 Å, 25 to 40 Å and 75 to 100 Å in width. The thinner fibrillar structures dominated the specimens from earlier stages of the precipitation procedure, while thicker ones predominated in the later samples. The sequential appearance of these structures and other observations suggested that they represented fibrils in different stages of development. These light and electron microscopic aspects of the precipitate have many points corresponding with those of the amyloid, although the identity between the two substances remains to be established. Moreover, the fibrillar structures could be produced in only 3 of 13 Bence Jones proteins treated in an identical fashion.

Footnotes

¹ These investigations were supported by grants from the United States Public Health Service, National Institute of Arthritis and Metabolic Diseases (AM-04599 and T1-AM-5285), from the General Clinical Research Centers Branch of the Division of Research Resources, National Institutes of Health (RR-533), from the Massachusetts Chapter of the Arthritis Foundation, from the Arthritis Foundation and from the John A. Hartford Foundation.

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