Abstract
1. 1. Crystalline Bacillus subtilis α-amylase, which has been reported to be a calcium metalloenzyme, also contains small amounts of zinc. Under normal conditions, this enzyme exists in the form of a dimer. 2. 2. Dissociation of the dimer takes place in the presence of metal-binding agents whereas dimerization is induced by zinc ions. One atom of zinc per molecule of dimer is taken up by the protein during dimerization and released as dissociation proceeds according to the following scheme: [Prot—Ca x—Zn—[Prot—Ca x] ▪2[Prot—Ca x]+Zn 3. 3. Formation of this zinc-protein complex appears to be peculiar to B. subtilis α-amylase. Intermolecular cross-linking under the influence of zinc has not been observed with α-amylases from human saliva, hog pancreas, or Aspergillus oryzae. 4. 4. Calcium ions do not induce dimerization of bacterial amylase.
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