Release of enzymes of intermediary metabolism from permeabilized cells: further evidence in support of a structural organization of the cytoplasmic matrix.
Cultured BSC-1 cells were exposed to the mild ionic detergent, Brij 58, and the time course of the release of three enzymes of intermediary metabolism (lactate dehydrogenase, aldolase, and creatine phosphokinase) was determined spectrophotometrically. Their release correlates well with the overall decrease in structural complexity of the cytoplasmic matrix. However, each of the three enzymes tested has its own characteristic time-dependent release profile, a result suggesting enzyme-specific variability in their association with the cytomatrix. Cells lysed for 5 min in Brij 58 and then transferred to detergent-free glycolysis medium were able to produce lactate from glucose, an observation consistent with the idea that all enzymes of the glycolytic pathway remained in the cytomatrix. These observations are consistent with a structural rather than viscous organization of the cytoplasm and suggest that cytoplasmic components other than cytoskeletal filaments are able to form parafilamentous, metastable complexes.
Department of Zoology, University of California, Berkeley 94720.
M
M
Schliwa
U
U
Euteneuer
K R
KR
Porter
D000818:Animals; D002460:Cell Line; D003402:Creatine Kinase / Q000378:metabolism*; D003593:Cytoplasm / Q000201:enzymology* / Q000648:ultrastructure; D003599:Cytoskeleton / Q000648:ultrastructure; D005634:Fructose-Bisphosphate Aldolase / Q000378:metabolism*; D006019:Glycolysis; D007770:L-Lactate Dehydrogenase / Q000378:metabolism*; D008854:Microscopy, Electron
D007770:L-Lactate Dehydrogenase; D003402:Creatine Kinase; D005634:Fructose-Bisphosphate Aldolase