The nuclear matrix of adrenal cells was isolated by using the methods
proposed by Commerford et al and Kaufmann et al for the liver nuclear
matrix isolation. Both methods permitted, to the best of our knowledge
for the first time, to prepare the nuclear matrix of a steroidogenic
cell and therefore to study some regulatory mechanisms governing stero
idogenesis. Commerford ef al's method retains nuclear envelope and so
produces a higher contamination; Kaufmann ef al's method presents a hi
gher purity since the nuclear envelope was removed by Triton X-100. No
RNase digestion has been employed for the isolation of the residual n
uclear matrices. Both methods however, permit the isolation of fractio
ns with a good morphology, retaining a reticular nucleolus, interchrom
atinic granules, and a fibrogranular scaffold extending from the nucle
olus to the nuclear lamina. The major peptides detected by 1-D SDS-PAG
E were 123, 56, 46 and 41 kDa; with both methods protein profiles were
similar. Identification of proteins by immunodetection reveals lamins
A and C, 80 and 65 kDa respectively; no labeling was found for actin
(45 kDa) and vimentin (57 kDa). In short, adrenal nuclear matrix was i
solated, Kaufmann et al's method being the method of choice.