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Protein Engineering, Vol. 13, No. 1, 1-4, January 2000
© 2000 Oxford University Press

Communications

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

Kazuo Masaki4, Ryusuke Masuda, Kenji Takase1, Keiichi Kawano2 and Katsutoshi Nitta3

Division of Biological Sciences, Graduate School of Science, Hokkaido University, Sapporo 060-0810, 1 Department of Biotechnology, National Institute of Agrobiological Resources, 2-1-2 Kannondai, Tsukuba, Ibaraki 305-8602 and 2 Faculty of Pharmaceutical Sciences, Toyama Medical and Pharmaceutical University, Toyama 930-0194, 4 Department of Insect Physiology and Behavior, National Institute of Sericultural and Entomological Science, Ministry of Agriculture, Forestry and Fisheries, Oowashi 1-2, Tsukuba, Ibaraki 305-8634, Japan

A domain-exchanged chimeric {alpha}-lactalbumin ({alpha}-LA), which consisted of the {alpha}-domain of human {alpha}-LA and the ß-domain of bovine {alpha}-LA, was constructed. Like native {alpha}-LA, the chimeric protein was in a molten globule state in the absence of Ca2+ at neutral pH and low salt concentration. The stability of the molten globule state of the constructed chimeric protein was identical to that of the recombinant human protein and was higher than that of the recombinant bovine protein. The stability of the molten globule state of {alpha}-LA is defined by the stability of the {alpha}-domain.


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