Parvalbumins (PVs) form a major part of the fish skeletal muscle sarcoplasm, and were identified as the major cross-reactive allergens in a variety of fish species. Therefore, the intake of fish or fish-linked products may cause serious clinical problems. It is known that the biochemical and structural characteristics of a protein play a central role in determining its potential functions. This study is sought to evaluate the stability of PV’s structure which would be the foremost reasons in keeping them responsive yet after cooking. Here, PVs obtained from a commonly consumed fish Channa marulius were used as the test protein. The protein, PV turned out to be fairly resistant to high temperatures (90 C) and set on in a typical single band of 10 kD in SDS-PAGE. This suggests that following heating only partial and/or reversible loss of PV structure occurred, which rendered it allergenic to predisposed individuals.