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Additional resources for Methods of Biochemical Analysis, Volume 21
Well-type NaI(T1) detector. They were then digested with a nitric-perchloric acid mixture (31). 0-ml aliquots were counted. The data are averages of determinations on duplicate samples. b The wheat was grown on a sand-soil mixture to which Na276SeOc had been added, as described in ref. 49a. 8 ppm. c The cut ends of the upper portions of Astragalus racernosus plants in the blossom stage of growth were dipped into a Na276SeO8solution for 1 hr and then in water under lights for 18 hr. After air drying, the leaves were finely ground with about 4 parts of leaves from untreated plants.
VESSEY selective aggregation of a portion of the smooth microsomes with MgC12 (48). 007M MgCI2. Centrifugation for 45 min at 102,OOOg in a No. 2 rotor yields one fraction of smooth microsomes as a pellet and another at the interface. The specific activity of glucose-6-phosphatase is different in these two subfractions of smooth microsomes (49). Unfortunately, however, the aggregating effect of MgCl2 cannot be reversed (%), and Mg2+ alters the kinetic properties of some microsomal enzymes (see Section 11).
E. SUBSTRATE FORMS Substrates for several tightly bound microsomal enzymes are nonpolar or amphipathic, and as a result have a strong affinity for the hydrophobic portions of the membrane. B) produce extensive alterations in microsomal structure, as indicated by turbidity changes, release of a TCA-soluble chromophore from the membrane, and activation of UDP glucuronyltransferase. Substrate-induced inactivation occurs in reactions utilizing acyl-CoA or lysophosphatides as substrates. The problem in this instance is related to the formation of micelles, which behave as detergents (65).