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A comparison of the ATPase activity of the glial cell fraction and the neuronal perikaryal fraction isolated in bulk from rat cerebral cortex 1
Author(s) -
Medzihradsky F.,
Nandhasri P. S.,
IdoyagaVargas V.,
Sellinger O. Z.
Publication year - 1971
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1971.tb00023.x
Subject(s) - medicine , chemistry , library science , computer science
SINCE SKOU (1957) first described a Na-K-activated, Mgdependent, and ouabain-sensitive adenosinetriphosphatase in crab nerve, considerable evidence has accumulated to implicate this enzyme in the transport of Na and K (see reviews by SKOU, 1965; and ALBERS, 1967). The activity of this ATPase is high in membrane preparations from various organs, the highest activity being that of membranes from nervous tissues (BONTING. SWON and HAWKINS, 1961). The enzyme is intimately associated with the membranes, but its solubilization and stabilization in solution have recently been accomplished (MEDZIHRADSKY, UINE and H o r n , 1967). Also, the regional distribution of Na-K ATPase has been mapped in the brain of the rabbit (HARMONY, URBL-HOLMGREN and URBAY, 1967) and the rhesus monkey (FAHN and G3d, 1968). In view of the cellular heterogeneity of brain and of unsettled questions concerning the role of glial cells and of their interrelations with neurons, we have compared the activities of Na-K ATPase and total ATPase of the neuronal perikaryal fraction and glial cell fraction obtained from cerebral cortex as two separate populations by a bulk-isolation procedure. In addition, we determined the intracellular distribution of these two enzymic activities in neuronal perikarya by the use of standard differential centrifugation techniques.