Isolation and characterization of the Neurospora crassa endoplasmic reticulum.
AUTOR(ES)
Borgeson, C E
RESUMO
The endoplasmic reticulum from Neurospora crassa was identified by monitoring the activity of the putative enzyme marker phosphatidylcholine glyceride transferase. After differential centrifugation of a cell homogenate, phosphatidylcholine glyceride transferase activity initially copurified with plasma membrane H+-ATPase. However, isopycnic centrifugation of the whole-cell homogenate on a linear sucrose gradient separated the two enzyme activities into different fractions. The lighter membrane fraction exhibited characteristics that have been associated with the endoplasmic reticulum in other organisms: (i) the inclusion of magnesium caused this light membrane fraction to shift to a higher density on the gradient; (ii) it was highly enriched in cytochrome c reductase, an endoplasmic reticulum marker in other systems; and (iii) the morphology of the light fraction with and without added magnesium was clearly distinguishable from that of the plasma membrane fraction by electron microscopy. A reinvestigation of the location of chitin synthetase confirmed its association with the plasma membrane fraction even after separation of the lighter fractions.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=215090Documentos Relacionados
- Coatomer-rich endoplasmic reticulum.
- Association of poliovirus proteins with the endoplasmic reticulum.
- "BFA bodies": a subcompartment of the endoplasmic reticulum.
- Competition between folding and glycosylation in the endoplasmic reticulum.
- Isolation and characterization of nuclei from Neurospora crassa.