Neuromuscular efficiency of the vastus lateralis and biceps femoris muscles in individuals with anterior cruciate ligament injuries

To analyze strength and integrated electromyography (IEMG) data in order to determine the neuromuscular efficiency (NME) of the vastus lateralis (VL) and biceps femoris (BF) muscles in patients with anterior cruciate ligament (ACL) injuries, during the preoperative and postoperative periods; and to compare the injured limb at these two times, using the non-operated limb as a control. EMG data and BF and VL strength data were collected during three maximum isometric contractions in knee flexion and extension movements. The assessment protocol was applied before the operation and two months after the operation, and the NME of the BF and VL muscles was obtained. There was no difference in the NME of the VL muscle from before to after the operation. On the other hand, the NME of the BF in the non-operated limb was found to have increased, two months after the surgery. The NME provides a good estimate of muscle function because it is directly related to muscle strength and capacity for activation. However, the results indicated that two months after the ACL reconstruction procedure, at the time when loading in the open kinetic chain within rehabilitation protocols is usually started, the neuromuscular efficiency of the VL and BF had still not been reestablished.

Kinetic study of crystallization of PHB in presence of hydroxy acids

Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)

Subcellular localization and kinetic characterization of a gill (Na +, K+)-ATPase from the giant freshwater prawn macrobrachium rosenbergii

The stimulation by Mg2+, Na+, K+, NH 4 +, and ATP of (Na+, K+)-ATPase activity in a gill microsomal fraction from the freshwater prawn Macrobrachium rosenbergii was examined. Immunofluorescence labeling revealed that the (Na +, K+)-ATPase α-subunit is distributed predominantly within the intralamellar septum, while Western blotting revealed a single α-subunit isoform of about 108 kDa M r. Under saturating Mg2+, Na+, and K+ concentrations, the enzyme hydrolyzed ATP, obeying cooperative kinetics with V M = 115.0 ± 2.3 U mg-1, K 0.5 = 0.10 ± 0.01 mmol L-1. Stimulation by Na+ (V M = 110.0 ± 3.3 U mg-1, K 0.5 = 1.30 ± 0.03 mmol L -1), Mg2+ (V M = 115.0 ± 4.6 U mg -1, K 0.5 = 0.96 ± 0.03 mmol L-1), NH4 + (V M = 141.0 ± 5.6 U mg -1, K 0.5 = 1.90 ± 0.04 mmol L-1), and K+ (V M = 120.0 ± 2.4 U mg-1, K M = 2.74 ± 0.08 mmol L-1) followed single saturation curves and, except for K+, exhibited site-site interaction kinetics. Ouabain inhibited ATPase activity by around 73 % with K I = 12.4 ± 1.3 mol L-1. Complementary inhibition studies suggest the presence of F0F1-, Na+-, or K +-ATPases, but not V(H+)- or Ca2+-ATPases, in the gill microsomal preparation. K+ and NH4 + synergistically stimulated enzyme activity (≈25 %), suggesting that these ions bind to different sites on the molecule. We propose a mechanism for the stimulation by both NH4 +, and K+ of the gill enzyme. © 2013 Springer Science+Business Media New York.