Abstract
The enzyme protochlorophyllide oxidoreductase (PCR) could be purified from Avena sativa plants by means of column chromatography and preparative gel electrophoresis. The amino acid composition of the protein was determined. The enzyme consists of 346 amino acids and has a molecular weight of approximately 37 800. Tryptophan is absent, and only one cysteine participates in the active site. The high content of basic amino acids explains the basic pI of approximately 8.5, observed by gel electrophoresis. The amino acid composition favours a theory explaining the observed association of the enzyme with the lipid environment of prolamellar bodies. Furthermore, the protein contains hydrophobic/hydrophilic amino acids in amounts similar as is known for intrinsic pigment binding proteins of the mature thylakoid membrane.
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