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|Type:||Artigo de periódico|
|Title:||Chemical Studies Of A Urinary Bence Jones Protein; Amino Acid Composition And Evidence Of A Covalently Bound Dimeric Structure|
|Abstract:||Bence Jones protein (JJO) typed as λ by specific immune sera was isolated from the urine of a paraproteinemic patient. Amino acid composition of BJP (JJO) showed a total number of 206 residues excluding tryptophan; the value found for half cystine determined as cysteic acid was 5 moles per mole of protein (taken as 22600). This result suggests that BJP (JJO) is arranged as a dimer in urine. Under 10% PAGE/SDS, native and reduced BJP (JJO) migrate as single bands. Native protein displays an electrophoretic mobility close to H chains (50 K) of reduced IgG1(JJO) λ and IgG1(GOB) k paraproteins; reduced BJP migrates as a typical lambda chain monomer (25 K) obtained from reduced IgG1(JJO) and IgG3(FKW) paraproteins. The data presented in compatible with the interpretation that BJP (JJO) in urine consists of two covalently bound homologous λ chains in a dimeric configuration.|
|Appears in Collections:||Unicamp - Artigos e Outros Documentos|
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