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. 1966 Feb;98(2):587–593. doi: 10.1042/bj0980587

Electrophoretic and other studies on haem pigments from Rhodopseudomonas palustris: Cytochrome 552 and cytochromoid c

R W Henderson 1, Diane D Nankiville 1
PMCID: PMC1264881  PMID: 5941351

Abstract

1. Cytochrome 552 and cytochromoid c were extracted from Rhodopseudomonas palustris cells, purified and obtained in crystalline form. 2. Extinction ratios and amino acid compositions of the two pigments are reported. 3. When subjected to starch-gel electrophoresis in borate buffer, pH8·8, each pigment migrated towards the cathode; oxidized cytochromoid c migrated more rapidly than its reduced form. 4. By a determination of electrophoretic mobilities in buffers of I0·1 by using the moving-boundary method, the isoelectric point of cytochrome 552 was found to be at pH10·6 and that of cytochromoid c at pH9·7. 5. As obtained, cytochrome 552 was non-autoxidizable; cytochromoid c was autoxidizable but became considerably less so on alkaline treatment. 6. Discussion of the results includes a consideration of the isoelectric points of the pigments in terms of their amino acid composition.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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