Sequential ordered mechanism for the sodium-glutamate transport in intestinal brush border membrane vesicles.

The glutamate/aspartate carrier localized in the brush-border membrane vesicles from enterocytes is known as a transport system catalyzing a sodium-substrate cotransport driven by the sodium gradient across the membrane. The kinetics of this transport system is studied by analogy with an enzymatic bi-substrate reaction. The results of this approach can be summarized as follows: (1) The dependence of the L-glutamate transport rate on the sodium concentration is sigmoidal, and the stoichiometry of the transport is 2 Na+/1 glutamate/1 carrier molecule. (2) The mechanism is sequential ordered, with L-glutamate binding after both the sodium cations. In addition, there is a very high degree of cooperativity between the two sodium binding sites.