Purification and characterization of four Bence-Jones proteins |
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| Authors: | M E Adams-Mayne B Jirgensons |
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| Affiliation: | 1. Center for Integrated Protein Science Munich at the Department Chemie, Technische Universität München, Lichtenbergstr, 4, 85748 Garching, Germany;2. Helmholtz Zentrum München, Institute of Structural Biology, Ingolstädter Landstr, 1, 85764 Neuherberg, Germany;3. Dipartimento di Bioscienze, Università degli studi di Milano, 20133 Milan, Italy;1. Center for Integrated Protein Science at the Department Chemie, Technische Universität München Lichtenbergstrasse 4, D-85747 Garching, Germany;2. Center for Integrated Protein Science at the Department Physik, Technische Universität München, James-Franck-Strasse 1, D-85748 Garching, Germany;3. Division of Protein Structural Biology, Institute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka 565-0871, Japan |
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| Abstract: | ![]()
Bence-Jones proteins from four multiple myeloma patients were isolated and studied with regard to homogeneity, composition, immunotype, and physical properties. One protein with molecular weight of 28,000 was unique in having two chains of unequal length. The protein from another patient was separated chromatographically into three components that differed in composition and properties. Two samples were homogeneous on chromatography, yet one of these was separable into three components in free boundary electrophoresis. The fact that the protein had a molecular weight of 56,000 and a C-terminal content of 2.8 serine residues per molecule indicated the possibility of three chains being associated in a molecule. The amino acid composition of these Bence-Jones proteins was compared with that of 15 other samples described in the literature. The report of van Eijk and Monfoort of a compositional difference between antigenic Types I and II was supported. |
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