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Journal article

Study by mutagenesis of the roles of two aromatic clusters of alpha-lactalbumin in aspects of its action in the lactose synthase system.

Abstract:

A new system for the bacterial expression of a variant of bovine alpha-lactalbumin has been developed. Eighteen mutant proteins containing single site substitutions in a cluster of predominantly aromatic residues adjacent to the cleft (aromatic cluster I) and in the hydrophobic box were expressed. The proteins were extracted from inclusion bodies and treated to generate native folding and disulfide bonds to provide appropriately folded protein samples for nine of the mutants. These were chara...

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Journal:
The Journal of biological chemistry
Volume:
269
Issue:
7
Pages:
5106-5114
Publication date:
1994-02-05
EISSN:
1083-351X
ISSN:
0021-9258
URN:
uuid:f6b56c9d-e564-4564-bf19-b808edb8e1b4
Source identifiers:
464794
Local pid:
pubs:464794

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