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Untersuchung der Bindung von Natrium‐ und Chlorid‐Ionen durch Casein mittels R ÖNTGEN ‐Strahlen‐ und Elektronen‐Beugung
Author(s) -
Gál S.,
Ludi A.,
Oswald H. R.,
Signer R.
Publication year - 1962
Publication title -
helvetica chimica acta
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.74
H-Index - 82
eISSN - 1522-2675
pISSN - 0018-019X
DOI - 10.1002/hlca.19620450309
Subject(s) - chemistry , casein , sodium , salt (chemistry) , aqueous solution , sodium salt , nuclear chemistry , inorganic chemistry , biochemistry , organic chemistry
Investigations by X‐ray and electron diffraction show that sodium chloride will be bound by casein, if the salt is added in aqueous solution to the protein and if the water is then removed under isothermal and nearly reversible conditions. This confirms earlier results obtained by water sorption measurements. The diffraction method is a simple and safe way for determining the maximum salt binding capacity of the protein. 90 to 95 models of NaCl are bound by 10 5 g of casein, which is more than 80% of the amount calculated from the amino‐acid composition of the protein.