Alteration of the substrate specificity of human lysozyme by site-specific intermolecular cross-linking.

doi:10.1016/0014-5793(94)01168-0

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Article

Alteration of the substrate specificity of human lysozyme by site-specific intermolecular cross-linking.

FEBS letters - 5 Dec 1994

Muraki M, Jigami Y, Harata K

Abstract excerpt

Human lysozyme dimers were prepared by the intermolecular cross-linking of the monomer that contained the mutation of either Arg41 to Cys or Ala73 to Cys with a divalent maleimide compound. Among the three kinds of possible dimers only R41C-R41C dimer, in which the two catalytic clefts can come c...

Topics

Alanine
Arginine
Base Sequence
Carbohydrate Sequence
Chitin
Circular Dichroism
Cross-Linking Reagents
Cysteine
Glucosides
Humans
Maleimides
Models, Molecular
Molecular Sequence Data
Muramidase
Mutagenesis, Site-Directed
Mutation
Oligosaccharides
Osmolar Concentration

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