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The interaction of the molecular chaperone α-crystallin with unfolding α-lactalbumin: a structural and kinetic spectroscopic study J Mol Biol, 318 (3) (2002), pp. 815-827 1:CAS:528:DC%2BD38Xks1KrsLw%3D 12054825 10.1016/S0022-2836(02)00144-4 View PDFView articleView in ScopusGoogle Sch...
Kulig M, Ecroyd H (2012) The small heat-shock protein αB-crystallin uses different mechanisms of chaperone action to prevent the amorphous versus fibrillar aggregation of α-lactalbumin. Biochem J 448(3):343–352. doi:10.1042/BJ20121187 Article CAS PubMed Google Scholar Laganowsky A, Benes...
The transitional pH's of lysozyme, cytochrome c, α-lactalbumin, and mouse milk casein in their reactions with salmine are 11.48 – 11.53, 11.36 – 11.40, 10.03 – 0.08, and 6.17 – 6.30, respectively. The equivalent combining weights, in the same order, are 69,000, 22,600, 25,600, ...