ISSN:
1750-3841
Source:
Blackwell Publishing Journal Backfiles 1879-2005
Topics:
Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
,
Process Engineering, Biotechnology, Nutrition Technology
Notes:
Conformational changes in bovine serum albumin (BSA), Ca++-free α-lactalbumin(apo-α-lac), and Ca++-saturated α-lactalbumin(holo-ct-lac) were examined via Fourier transform infrared (FTIR) spectroscopy after pressure treatment up to 1270 MPa. BSA showed minimal irreversible secondary structural changes with pressurization, showing a slight loss of β-sheet structure in favor of α-helix. Apo-α-lac underwent major irreversible changes and exhibited infrared bands characteristic of aggregation upon decompression. Holo-α-lac showed extensive resistance to high pressure with no major structural changes. The rich disulfide content in BSA and the presence of Ca++ in holo-α-lac may play important roles in stabilizing these proteins against pressure denaturation.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1111/j.1365-2621.2002.tb10285.x
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