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- W1546543246 abstract "The stability of the methionine 80 sulfur–heme iron bond of ferricytochrome c (cyt c) in its complex with heparin has been studied by absorption spectroscopy in the alkaline pH region at temperatures of 20–80°C and low ionic strength. According to spectral data, the midtransition temperature (T1/2) of the cleavage of the sulfur–iron bond was 57.5±0.5 and 52.5±0.5°C for cytochrome c and cytochrome c–heparin complex, respectively, at neutral pH. The increasing in pH caused an expressive fall of cyt c transition temperature while the T1/2 for cyt c in its complex with heparin was constant and from pH>7.7, this value was higher than that for the free cyt c. Addition of heparin to cyt c evoked a moderate increase of 695 nm band intensity at neutral or slightly alkaline pH. It was shown that heparin stabilises the conformation of cyt c in state III (the Met 80–heme iron bond is presented) in alkaline pH region and physiological temperature range." @default.
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- W1546543246 date "2001-07-01" @default.
- W1546543246 modified "2023-10-17" @default.
- W1546543246 title "Conformational stability of ferricytochrome c near the heme in its complex with heparin in alkaline pH" @default.
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- W1546543246 doi "https://doi.org/10.1016/s0144-8617(00)00253-8" @default.
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