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Título

Structural changes in cod myosin after modification with formaldehyde or frozen storage

Autor Careche, Mercedes ; Li-Chan, E
Palabras clave Myosin
Frozen storage
Formaldehyde
Raman
Cod
Fecha de publicación 1997
EditorWiley-VCH
Citación Journal of Food Science 62: 717- 723 (1997)
ResumenStructural changes in cod myosin after formaldehyde (FA) addition with and without subsequent freezing at - 18°C were examined by Raman spectroscopy, ANS hydrophobicity, solubility and SDS-PAGE profiles. Protein solubility decreased by >90%, whereas ANS fluorescence showed little change, possibly due to a balance between soluble and insoluble fractions differing in exposed hydrophobicity. SDS-PAGE showed irreversible insolubilization at increasing FA concentration, especially after frozen storage. Raman spectral analysis indicated a change in secondary structure of aquacide concentrated myosin preparations, from 95% α-helix in the control (no FA) to 60% after 12 mM FA treatment. Changes in vibrational modes assigned to aliphatic residues suggested involvement of hydrophobic interactions after FA addition or frozen storage.
URI http://hdl.handle.net/10261/101982
DOI10.1111/j.1365-2621.1997.tb15443.x
Identificadoresdoi: 10.1111/j.1365-2621.1997.tb15443.x
issn: 0022-1147
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