Plantar loading reflects ulceration risks of diabetic foot with toe deformation.

Diabetes has been one of the most common chronic diseases all over the world. The purpose of this study was to quantitatively assess the foot loading characteristics of diabetic patients with fifth-toe deformity through a comparative analysis with diabetic patients with healthy and normal feet. Six neuropathic diabetic female subjects with the fifth-toe deformation and six age-matched neuropathic diabetic controls without any feet deformities participated in the walking test. Dynamic barefoot plantar pressure was measured with Novel EMED force plate. Peak pressure and pressure-time integral for all 7 foot regions (rearfoot, midfoot, lateral forefoot, central forefoot, medial forefoot, great toe, and other toes) were collected. Peak pressure was significantly higher in the patients with toe deformity in rearfoot, central forefoot, and great toe regions compared with the control group. Meanwhile, loading sustaining period extended longer in great toe region of deformed group than in that of the control group, and the center of pressure was nearly in the big toe region during toe offstage. Diabetic patients with fifth-toe deformity could have plantar contact area reduction in the other toes part and increased loading to the great toe part. The result showed that fifth-toe deformity was associated with potential ulceration risk especially in hallux region.

The Kinematics and Kinetics Analysis of the Lower Extremity in the Landing Phase of a Stop-jump Task.

Large number of studies showed that landing with great impact forces may be a risk factor for knee injuries. The purpose of this study was to illustrate the different landing loads to lower extremity of both genders and examine the relationships among selected lower extremity kinematics and kinetics during the landing of a stop-jump task. A total of 35 male and 35 female healthy subjects were recruited in this study. Each subject executed five experiment actions. Lower extremity kinematics and kinetics were synchronously acquired. The comparison of lower extremity kinematics for different genders showed significant difference. The knee and hip maximum flexion angle, peak ground reaction force and peak knee extension moment have significantly decreased during the landing of the stop-jump task among the female subjects. The hip flexion angle at the initial foot contact phase showed significant correlation with peak ground reaction force during landing of the stop-jump task (r=-0.927, p<0.001). The knee flexion angle at the initial foot contact phase had significant correlation with peak ground reaction force and vertical ground reaction forces during landing of the stop-jump task (r=-0.908, p<0.001; r=0.812, P=0.002). A large hip and knee flexion angles at the initial foot contact with the ground did not necessarily reduce the impact force during landing, but active hip and knee flexion motions did. The hip and knee flexion motion of landing was an important technical factor that affects anterior cruciate ligament (ACL) loading during the landing of the stop-jump task.

Isolation and characterization of cytochrome C1 from photosynthetic bacterium Rhodopseudomonas sphaeroides R-26.

Cytochrome c1 of photosynthetic bacterium R. sphaeroides R-26 has been purified from isolated cytochrome b-c1 complex to a single polypeptide, using a procedure involving Triton X-100 and urea solubilization, calcium phosphate column chromatography and ammonium sulfate fractionation. The purified protein contains 30 nmoles heme per mg protein and has an apparent molecular weight of 30,000, as determined by sodium dodecylsulfate polyacrylamide gel electrophoresis. Bacterial cytochrome c1 is soluble in aqueous solution in the absence of detergent and has spectral characteristics similar to mammalian cytochrome c1. The amino acid compositions of these two proteins, however, are not comparable.

Characterization of purified cytochrome b-c1 complex from Rhodopseudomonas sphaeroides R-26.

A highly purified cytochrome b-c1 complex from Rhodopseudomonas sphaeroides R-26 was isolated by a procedure involving Triton X-100 solubilization, calcium phosphate column chromatography, and ammonium sulfate fractionation. The purified enzyme complex contains, in nanomoles/mg of protein, cytochrome b, 8.3; cytochrome c1, 8.3; iron-sulfur protein, 15; phospholipids, 182; and ubiquinone, 5. Four major polypeptides with apparent molecular weights of 48,000, 30,000, 24,000, and 12,000 were detected in the sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The Mr = 48,000 and 30,000 proteins are cytochromes b and c1, respectively. The enzyme complex catalyzes electron transfer from ubiquinol to cytochrome c with a specific activity of 12.6 mumol of cytochrome c reduced per min/mg of protein at 23 degrees C. This is lower than that of the mitochondrial enzyme, although both systems have similar essential redox components and a similar Km for ubiquinol. The activity is fully sensitive to antimycin A and 5-n-undecyl-6-hydroxy-4, 7-dioxobenzothiazole. The enzyme complex is stable at neutral pH and at lower temperatures, but became less stable when the incubation temperature was raised. At 37 degrees C, the half-life is 15 min. The enzymatic activity was insensitive to treatment with N',N'-dicyclohexylcarbodiimide. No p-chloromercuriphenylsulfonate-alkylable sulfhydryl groups were detected. The major phospholipids associated with the purified enzyme complex are phosphatidylcholine, phosphatidylethanolamine, and phosphatidylglycerol with molar per cent distributions of 25, 21, and 35, respectively. About 60% of the enzymatic activity was abolished upon treatment with phospholipase A2. The phospholipase A2-inactivated activity can be partially restored by the addition of EDTA followed with phospholipids prepared from either the cytochrome b-c1 complex of the same source or a mixture of phosphatidylglycerol and asolectin.(ABSTRACT TRUNCATED AT 250 WORDS)