Studies on cytochrome c-heparin interactions by differential scanning calorimetry
Keyword(s):
The effects of heparin on the thermotropic properties of ferricytochrome c have been studied using high-sensitivity differential scanning calorimetry. Saturating concentrations of heparin at low ionic strength induced an important shift of the transition temperature Tm from 84.1 degrees C to 59.8 degrees C. This was accompanied by unusually large cooperativity of thermal denaturation of this complex, indicating strong intermolecular interactions between protein molecules. The destabilization of cytochrome c when mixed with heparin was not observed at high ionic strength, under which conditions complex was not formed.
2010 ◽
Vol 288
(18)
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pp. 1687-1696
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1989 ◽
Vol 984
(2)
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pp. 214-224
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2003 ◽
Vol 252
(1-2)
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pp. 235-240
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2011 ◽
Vol 34
(1)
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pp. 45-51
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2006 ◽
Vol 322
(1-2)
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pp. 113-118
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1988 ◽
Vol 151
(1)
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pp. 429-434
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Keyword(s):
Reversible and non-reversible thermal denaturation of lysozyme with varying pH at low ionic strength
2013 ◽
Vol 1834
(10)
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pp. 2064-2070
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