The incorporation of isotope from [2-
14
C]ethanol by cultures of the Brannon no. 1 strain of
Chlorella vulgaris
, growing on ethanol aerobically in the dark, was consistent with the operation of the tricarboxylic acid and glyoxylate cycles. Results obtained with [l-
14
C]acetate, added to similar cultures growing on glucose in the dark or on carbon dioxide in the light, indicated that the glyoxylate cycle did not function under these conditions. However, one of the key enzymes of this cycle, isocitrate lyase, was present in large amounts in extracts of this organism under all conditions of growth; in contrast, isocitrate lyase was inducibly formed by
Chlamydomonas reinhardii
prior to growth on acetate. No obvious dysfunction of the tricarboxylic acid cycle, which might necessitate the activity of isocitrate lyase during growth on other than C
2
-compounds, was detected in the Brannon no. 1 strain, nor were differences observed between the properties of the enzyme purified from cells grown on acetate and on glucose. But, whereas isocitrate lyase was wholly found in a soluble fraction of the organism after growth on glucose or on carbon dioxide, acetate-grown cells contained a major portion of their isocitrate lyase in a dense, particulate fraction. The Brannon no. 1 strain of
Chlorella
excreted labelled glycollate during growth in the dark on glucose in the presence of sodium [
14
C]bicarbonate, but ceased to do so after transfer to acetate growth medium. The Pearsall’s strain of
Chlorella
, which does not form isocitrate lyase during growth on glucose, did not excrete labelled glycollate under these conditions. These results suggest that the Brannon no. 1 strain of
Chlorella
contained an active isocitrate lyase under all conditions of growth, but that this enzyme participates in the glyoxylate cycle only when it is incorporated into a particulate structure.
Autophagic Machinery of Plant Peroxisomes
