The functioning of the Golgi complex in protein intracellular transport is most simply understood in terms of its being composed of a sequence of functionally distinct subcompartments. For example, the influence of perturbation of cellular Na+-K+ balance on the transport of secretory and membrane glycoproteins is to greatly slow their passage from relatively proximal to relatively distal subcompartments. To further the understanding of the nature of these subcompartments a rat IgM myeloma has been subjected to analytical subcellular fractionation. Fractions selectively enriched in distinct Golgi-associated activities have been prepared and their membrane proteins compared with those of rough microsomal fractions. The subfractionation is extensive and suggests the possibility of obtaining well resolved Golgi subfractions. Myeloma cells stained intracellularly with Concanavalin A- and wheatgerm agglutinin--peroxidase conjugates show distinct labelling patterns. Concanavalin A stains the entirety of the rough endoplasmic reticulum as well as the proximal face of the Golgi stack. Wheatgerm agglutinin stains the distal face of the stack of Golgi cisternae. The staining patterns are not due to immunoglobulin as they are also observed in myeloma variants that fail to synthesize immunoglobulin.