Kristallisierte Leucinaminopeptidase aus Rinderaugenlinsen. Physikalische Konstanten, III: Optische Rotationsdispersion

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Abstract
Leucine aminopeptidase from bovine lens was prepared and crystallized by 2 different methods. The 2 preparations were comparded by optical rotatory dispersion and the rotation at the negative Cotton peak; the helix content was measured to about 20% and compared with the permitted maximum calculated from the amino acid analysis. The change in the helix percentage under the influence of sodium dodecyl sulphate (1 mg/mg protein), 8M urea, [beta]-mercaptoethanol in 8M urea solution, and [beta]-chloroethanol was studied. The results show the linkage of the subunits is mediated by disulphide bridges, which are buried in the molecule in such a way that denaturation is necessary to make them available to the reducing agent. The helical region in the polypep-tide chains of the subunits is probably bridged by a disulphide linkage, since [beta]-chloroethanol hardly affects the ability of the coiled region to form the maximal possible helix.

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