Abstract
Quasicrystalline protein from Neurospora crassa, prepared by three different methods, was analyzed for the presence of free N-terminal groups. It was found that quasicrystalline protein prepared with alkali treatment, but not material prepared without alkali, had free terminal amino groups. It was concluded that use of alkali to digest uv-absorbing material normally associated with quasicrystalline protein also caused hydrolysis of peptide bonds. An alternative method using short exposures to perchloric acid is suggested as an alternative step for the preparation of this protein fraction.
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