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. 1998 Mar;116(3):1029–1036. doi: 10.1104/pp.116.3.1029

Figure 2.

Figure 2

Internal amino acid (aa) sequences of the NFORase purified from spinach leaf PM vesicles. Frozen PM vesicles were thawed and diluted with buffer with low ionic strength and low osmotic potential and then pelleted by centrifugation. Enzyme 1 was purified from the pellet after CHAPS solubilization, and enzyme 2 was purified from the supernatant containing proteins released by the freezing-thawing procedure and hypo-osmotic shock. Search for homologous internal sequences in the Swiss-Prot databank identified highly homologous sequences in monodehydroascorbate radical reductases in three different species. Numbers on the right are the amino acid positions of the highly homologous sequences in the known MDA reductases. Bold letters indicate identity.