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- W2005481946 abstract "The amounts of the larval cuticular proteins bound non-covalently by Scylla serrata chitin depend on both the pH and the ionic strength of the solution. Binding is greatest at the isoelectric point of the protein and at low salt concentrations. The binding of some proteins is partly reversible and complete removal of bound protein requires solvents able to break hydrogen bonds. The cuticular proteins are heterogeneous and some minor components of low molecular weight are not bound by the chitin. Those components which are bound have similar affinities for the chitin. Although crab chitin can bind 2.4 times its weight of Calliphora cuticular protein the binding of proteins in insect cuticle is less as only the outer surfaces of the chitin microfibrils are accessible to protein and the non-covalent binding is further limited by covalently bound protein. It is likely that chitin in the cuticle is saturated with protein. Chemical modifications of the proteins lead to the conclusion that the non-covalent binding between the chitin and the proteins is non-specific." @default.
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- W2005481946 date "1978-01-01" @default.
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- W2005481946 title "The non-covalent binding of two insect cuticular proteins by a chitin" @default.
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- W2005481946 doi "https://doi.org/10.1016/0020-1790(78)90021-5" @default.
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