Determination of the characteristics, properties and homogeneity of rat brain microsomes. Binding of lactate dehydrogenase, malate dehydrogenase and 5' nucleotidase to microsomal membranes.
Quantitatively, the amount of microsomes obtained using dimethyl sulfoxide is larger than that obtained from sucrose solutions (Centelles, Franco & Bozal (1986) Biol. Chem. Hoppe Seyler 367, 461-475). In this paper it is demonstrated that from a qualitative point of view they appeared to be indistinguishable with respect to molecular characteristics. Thus, both types of microsomes had the same behaviour in experiments of isopicnic ultracentrifugation with Percoll, isoelectric focusing and gel permeation. In these experiments, the 5'-nucleotidase, lactate dehydrogenase and malate dehydrogenase activities bound to the microsomal fraction were also studied. Lactate and malate dehydrogenase activities were always found in free and membrane-bound form. In contrast, 5'-nucleotidase activity was always encountered bound to microsomal membranes.
Franco
R
R
Departament de Bioquimica i Fisiologia, Facultat de Quimica, Universitat de Barcelona, Spain.
Centelles
J J
JJ
Canela
E I
EI
D015720:5'-Nucleotidase; D000818:Animals; D001921:Brain / Q000201:enzymology*; D002500:Centrifugation, Isopycnic; D002850:Chromatography, Gel; D066298:In Vitro Techniques; D007525:Isoelectric Focusing; D007770:L-Lactate Dehydrogenase / Q000378:metabolism*; D008291:Malate Dehydrogenase / Q000378:metabolism*; D008854:Microscopy, Electron; D008861:Microsomes / Q000201:enzymology; D009708:Nucleotidases / Q000378:metabolism*; D051381:Rats; D011919:Rats, Inbred Strains
D007770:L-Lactate Dehydrogenase; D008291:Malate Dehydrogenase; D009708:Nucleotidases; D015720:5'-Nucleotidase