The Binding of the "Structural" Zinc Ions in Crystalline Insulin.

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Abstract
The site of binding of zinc in crystalline insulin has been investigated by determinations of the molecular weight of insulin which has been substituted on the N-terminal amino groups by phenyl-isocyanate and of insulin in which all carboxyl groups have been methylated. It is shown that the N-terminal amino groups are essential for the zinc-binding capacity of insulin whereas the carboxyl groups are without importance as regards the binding of zinc to insulin. In conclusion it is made probable that the zinc is attached to the N-terminal amino group of phenylalanine.
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