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Refolding and disulfide bond formation in reduced denatured bovine alpha-lactalbumin is shown to be Ca2+-dependent. Whereas in the absence of Ca2+ only about 2% of the native active protein is regenerated, in the presence of Ca2+, almost quantitative renaturation is obtained. A close coupling between Ca2+-binding and native disulfide bond formation is also indicated by spontaneous disulfide scrambling in the apoprotein in the presence of low concentrations of thiols. This phenomenon is not found in other disulfide-containing proteins including the homologous chicken lysozyme. It is proposed that the alpha-lactalbumin Ca2+-binding site has the in vivo function of imposing Ca2+ regulation on the folding of nascent alpha-lactalbumin and thereby on lactose synthesis.
K R Rao, and
K Brew
April 2004,
The Journal of biological chemistry,
K R Rao, and
K Brew
July 1998,
Protein science : a publication of the Protein Society,
K R Rao, and
K Brew
September 2015,
Proceedings of the National Academy of Sciences of the United States of America,
K R Rao, and
K Brew
September 1999,
Proceedings of the National Academy of Sciences of the United States of America,
K R Rao, and
K Brew
January 1996,
Biochemistry,
K R Rao, and
K Brew
November 2008,
Biochemistry,
K R Rao, and
K Brew
April 1993,
Biochemistry,
K R Rao, and
K Brew
December 2020,
Molecules (Basel, Switzerland),
K R Rao, and
K Brew
May 1992,
The EMBO journal,
K R Rao, and
K Brew
September 1990,
Biochemistry,
