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- G. G. Glenner
- National Institutes of Health, Bethesda, Maryland 20014
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- D. Ein
- National Institutes of Health, Bethesda, Maryland 20014
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- E. D. Eanes
- National Institutes of Health, Bethesda, Maryland 20014
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- H. A. Bladen
- National Institutes of Health, Bethesda, Maryland 20014
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- W. Terry
- National Institutes of Health, Bethesda, Maryland 20014
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- D. L. Page
- National Institutes of Health, Bethesda, Maryland 20014
抄録
<jats:p>"Amyloid" fibrils have been created from some human Bence Jones proteins by proteolytic digestion under physiologic conditions. These fibrils with an antiparallel, β-pleated sheet conformation consist of only a portion of the variable region of the immunoglobulin light polypeptide chain and share the physical properties of amyloid fibrils. The relation between amyloidosis and immunoglobulins is thus more firmly established and a pathogenetic mechanism for amyloid fibril formation is suggested.</jats:p>
収録刊行物
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- Science
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Science 174 (4010), 712-714, 1971-11-12
American Association for the Advancement of Science (AAAS)
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キーワード
詳細情報 詳細情報について
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- CRID
- 1361981468818910464
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- NII論文ID
- 30020501352
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- ISSN
- 10959203
- 00368075
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- データソース種別
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- Crossref
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