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- W31955519 abstract "Publisher Summary This chapter discusses the biochemical properties of the enigmatic chloroplast cytochrome b -559. The maximum heme content of the cytochrome that has been obtained is 58 nmoles heme/mg protein. In the early preparations, the heme content was much lower. The heme of cytochrome b -559 is more labile than that of cytochrome b 6 and it is difficult to stain the heme on a denaturing gel, even lithium dodecyl sulfate gel run at 0°C. As soon as the denaturing conditions of the gel are sufficient to allow the b -559 to penetrate, the heme is often lost. When the heterogeneity in the N-terminal residues in that preparation is considered, it appears likely that their heme content of one heme per 46,000 polypeptide molecular weight was a result of heme dilution because of heme loss and possibly contamination by other proteins. If high and low potential b -559 are derived from the same molecule, there should be no distinction in the purified cytochrome. However, one cannot eliminate the possibility that 20% of the cytochrome b -559 in the membrane is not extractable and that the unextractable component is phosphorylated." @default.
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- W31955519 date "1983-01-01" @default.
- W31955519 modified "2023-09-26" @default.
- W31955519 title "BIOCHEMICAL PROPERTIES OF THE ENIGMATIC CHLOROPLAST CYTOCHROME b-559: PARTIAL AMINO ACID SEQUENCE OF A PURIFIED b-559 POLYPEPTIDE AND STUDIES ON THE IDENTITY OF THE Mr = 9,000 PHOSPHOPROTEIN" @default.
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- W31955519 doi "https://doi.org/10.1016/b978-0-12-372360-4.50020-1" @default.
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