The polypeptide composition of purified mitochondria isolated from pea epicotyls was studied by one‐ and two‐dimensional electrophoresis. It was shown that two‐dimensional electrophoresis was necessary to clearly resolve polypeptides of molecuar weights ranging from 50 000 to 60 000. Mitochondria were fractionated into a soluble fraction corresponding to the matrix and an insoluble fraction containing membrane components. Spots characteristic of one or the other fraction were thus localized on the two‐dimensional gel map of whole mitochondria. In addition, a comparison was made of polypeptide composition in mitochondria isolated from etiolated and green leaves. It was shown that mitochondria from photosynthetic tissue differ from those on non‐photosynthetic tissue by quantitative and qualitative changes of their polypeptide composition. The most characteristic changes in green leaves are the loss of one polypeptide (Mr 35 000 and pI 6.3) and the quantitative increase of four other spots. These spots belong to the matrix compartment. Their apparent molecular weights are 97 000, 51 000, 43 000 and 15 000. Conversion of glycine to serine during the photorespiration process being characteristic of mitochondria from photosynthesizing tissue, we suggest that these spots could correspond to subunits of the glycine decarboxylase multienzyme complex.
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Rémy et al. (1987) studied this question.
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