Stability of the molten globule state of a domain-exchanged chimeric protein between human and bovine alpha-lactalbumins

Authors
Masaki, K Masuda, R Takase, K Kawano, K Nitta, K
Citation
K. Masaki et al., Stability of the molten globule state of a domain-exchanged chimeric protein between human and bovine alpha-lactalbumins, PROTEIN ENG, 13(1), 2000, pp. 1-4
Citations number
17
Categorie Soggetti
Biochemistry & Biophysics
Journal title
PROTEIN ENGINEERING
ISSN journal
02692139 → ACNP
Volume
13
Issue
1
Year of publication
2000
Pages
1 - 4
Database
ISI
SICI code
0269-2139(200001)13:1<1:SOTMGS>2.0.ZU;2-Q
Abstract
A domain-exchanged chimeric alpha-lactalbumin (alpha-LA), which consisted o f the a-domain of human alpha-LA and the beta-domain of bovine alpha-LA, wa s constructed. Like native alpha-LA, the chimeric protein was in a molten g lobule state in the absence of Ca2+ at neutral pH and low salt concentratio n, The stability of the molten globule state of the constructed chimeric pr otein was identical to that of the recombinant human protein and was higher than that of the recombinant bovine protein, The stability of the molten g lobule state of alpha-LA is defined by the stability of the alpha-domain.