Title : Structural characterization of the disulfide folding intermediates of bovine alpha-lactalbumin.

Pub. Date : 1993 Apr 13

PMID : 8466909






5 Functional Relationships(s)
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1 Structural characterization of the disulfide folding intermediates of bovine alpha-lactalbumin. Disulfides lactalbumin alpha Bos taurus
2 Specific three- and two-disulfide intermediates that accumulate transiently during reduction of the disulfide bonds of Ca(2+)-bound bovine alpha-lactalbumin have been trapped, isolated, and characterized. Disulfides lactalbumin alpha Bos taurus
3 Specific three- and two-disulfide intermediates that accumulate transiently during reduction of the disulfide bonds of Ca(2+)-bound bovine alpha-lactalbumin have been trapped, isolated, and characterized. Disulfides lactalbumin alpha Bos taurus
4 The remaining native disulfide bonds in the two partially reduced derivatives of alpha-lactalbumin are stable only when the proteins are in a Ca(2+)-bound state. Disulfides lactalbumin alpha Bos taurus
5 The native structure of alpha-lactalbumin appears to be split by selective disulfide bond cleavage into at least one subdomain, which retains the Ca(2+)-binding site. Disulfides lactalbumin alpha Bos taurus