In the human body skeletal muscle is the largest store of glutamine, an important amino-acid in whole body nitrogen balance. Glutamine transport was measured in purified human skeletal muscle sarcolemmal vesicles (HMSV). The activity of sarcolemmal marker enzymes (K(+)-stimulated nitrophenylphosphatate (KpNPPase) and 5'-nucleotidase) was increased approximately 14-fold in the sarcolemmal fraction (SF) compared to the crude muscle homogenate (CH). Glutamine transport in HMSV was Na(+)-dependent (initial rate of 1 muM glutamine in the presence of 0.1 M NaCl = 7 (+/- 1.7) x 10(-3) pmol.mg(-1) protein.s(-1) compared to 1.5 (+/- 0.3) x 10(-3) pmol mg(-1) protein.s(-1) in the presence of 0.1 M Choline Cl). The rate of glutamine uptake into HMSV was increased in the presence of an inside negative membrane potential.
Studies of glutamine uptake across human skeletal sarcolemma. Publishing Authors By Initials