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HERO ID
8703602
Reference Type
Journal Article
Title
Conformation and immunochemistry of parvalbumin III from Pike white muscle. Modification of the arginine residue with 1,2-cyclohexanedione
Author(s)
Gosselin-Rey, C; Bernard, N; Gerday, C
Year
1973
Volume
303
Issue
1
Page Numbers
90-104
Language
English
DOI
10.1016/0005-2795(73)90151-7
Abstract
1. 1. The single arginine residue of parvalbumin III from Pike white muscle has been modified with 1,2-cyclohexanedione. The purity of the modified protein is established by amino acid analysis, immunoelectrophoresis and peptide mapping. 2. 2. The immunochemical study indicates the loss of at least two antigenic determinants together with conformational changes in the molecule. 3. 3. A reduced percentage of α helicity is demonstrated by ORD and CD measurements. 4. 4. The Ca2+ associated with the modified protein is reduced to 50-25% of the amount in the native parvalbumin. 5. 5. It is concluded that the arginine residue plays a key role in the tertiary structure of the molecule. 1973.
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