On the cryoaggregation of bovine serum albumin
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It has often been observed that freezing plant tissues results in denaturation and precipitation of the plant proteins. The low temperature denaturation of proteins has been termed cryodenaturation, and, it is similarly fitting to describe the precipitation as cryoaggregation. Thus, it was felt important to investigate the changes which occur during the freezing of protein solutions. Such a system may be used as a model, and may feasibly serve as a tool in the eventual solution to the mystery of frost hardiness in plants. It is the purpose of this study, then, to investigate as many aspects as possible of the principles involved in the cryoaggregation of proteins. Bovine serum albumin was chosen for the model system due to its availability in extremely pure form. The changes which occurred on freezing of both the native disulfide form and the reduced sulfhydryl form of the protein were studied in an attempt to learn the nature of the protein interactions which occur during cryo aggregation.
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This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivs 3.0 License.