Secondary structural change of bovine serum albumin in thermal denaturation up to 130 degrees C and protective effect of sodium dodecyl sulfate on the change.

The secondary structure of bovine serum albumin (BSA) was first examined in the thermal denaturation up to 130 degrees C. The helicity (66%) of the protein decreased with rise of temperature. Half of the original helicity was lost at 80 degrees C, but the helicity of 16% was still maintained even at 130 degrees C.