Hydrophobic profiling of heated and unheated Leghemoglobin, Myoglobin, Cytochrome c and Hemoglobin proteins in differential pH conditions

Rittik Kumar Ghosh, Turban Kar, Pijush Basak, Maitree Bhattacharyya

Abstract


Surface hydrophobicity of leghemoglobin (Lb),
myoglobin (Mb) ,cytochrome c (Cyt C) and hemoglobin (Hb)
under heated (80 °C for 30 min.) and unheated conditions and at
varying pH values (3.0, 5.0, 7.0, and 9.0) were measured using
ANS, CPA, and PRODAN. Hydrophobicity was lower at pH 9.0,
5.0 and 7.0 for all proteins measured by PRODAN, for ANS and
for CPA respectively. Lb shows maximum hydrophobic nature
with ANS and CPA may and less with PRODAN compared to
other heme proteins, indicating that Lb favor less ionic
interaction. These results suggest that the presence of a
permanent charge of fluorescent probes can affect protein
hydrophobicity values measured under various pH conditions for
Lb.

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