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|Type:||Artigo de periódico|
|Title:||The Interchain Disulphide Bridge Of Bence Jones (jjo) Protein: Isolation And Characterization Of The C-terminal End, Cysteine Containing, Tryptic And Peptic-tryptic Peptides Which Stabilize The Dimeric Configuration|
|Abstract:||Reduction and radioactive alkylation followed by enzymatic digestion of purified urinary Bence Jones (JJO) protein led, after purification procedures, to the isolation of the C terminal and cysteine containing peptic Pro-Thr-Glu-*CMCys-Ser pentapeptide and the tryptic Thr-Val-Ala-Pro-Thr-Glu-*CMCys-Ser octapeptide which are characteristic of λ chains. These peptides were purified after vertical high voltage electrophoresis of whole digests applied on chromatographic Whatman 3MM paper after successive runs at pH 3.5, 6.5 and 2.1. Characterization was obtained from amino acid composition, sequence determination and homology studies of the radioactive material contained in ninhidrin positive bands. The results presented chemically classify BJP (JJO) as a lambda protein and confirm the primary structure around the interchain disulphide bridge that stabilizes its dimeric configuration.|
|Appears in Collections:||Unicamp - Artigos e Outros Documentos|
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