Effect of limited knee-flexion range on peak hip moments of force while transferring from sitting to standing

The hypothesis that limiting the knee-flexion range increases the peak hip-extension moment while transferring from sitting to standing was tested by filming (100 fps) ten normal human volunteers. With the knees flexed 105 degrees from full extension (0 degrees) the mean (+/- 1 S.D.) peak hip-extension moment was 142 (+/- 37) Nm. With the knees flexed only 75 degrees subjects threw their arms and trunks forward to a greater extent, with a peak moment of 253 (+/- 65) Nm (p less than 0.0001). If the peak moments rise to a similar degree in patients with arthritis and limited knee-flexion range, they may accelerate hip joint damage or the loosening of hip endoprostheses.     

The interaction of 1-anilino-8-naphthalenesulfonate with thyroid lipids and membranes: A nuclear magnetic resonance study

The proton magnetic resonance (PMR) spectra of thyroid cell membranes and their total lipid extracts, in the presence of 1-anilino-8-naphthalenesulfonate (ANS), have been studied. The addition of ANS causes a shifting of the head group PMR signal, a splitting of the signal into two components and an increase in total spectral intensity. The data suggest that ANS interacts with phospholipid in the membrane as it does in total lipid vesicles. Evidence is also presented for the removal of lipids from the membrane, by ANS, and the subsequent formation of micelles. The membrane results are compatred with our earlier work on the interaction of ANS with egg phosphatidycholine (P.C.) vesicles and the results are used in explaining the inhibition of iodide transport in isolated thyroid slices.     

Aerobic photolysis of alkylcobalamins: quantum yields and light-action spectra

Quantum yields (φ) for the aerobic photolysis of 5′-deoxyadenosylcobalamin (dAB₁₂), methylcobalamin (MeB₁₂), propylcobalamin (PrB₁₂), and ethylcobalamin (EtB₁₂) were determined as a function of the irradiation wavelength. φ Determinations were made for both the base-on and base-off forms of each compound (except base-off dAB₁₂) at incident wavelengths from 250 nm to 570 nm. As a rule, the φs were high (0.1–0.5) and they varied significantly with respect to the irradiation wavelength. In general, each alkylcobalamin at pH 7.0 displayed a quantum yield spectrum distinct from its base-off form at pH 1.0. Across most of the spectrum, the φs of the base-off form were appreciably smaller than the base-on φs of the same compound. An exception to this generality was MeB₁₂ for which the φs at pH 1.0 were about the same as, or slightly greater above 450 nm than those at pH 7.0. At pH 7.0 and in the visible region the trend of the φs was dAB₁₂ < MeB₁₂ < PrB₁₂ < EtB₁₂. Under neutral conditions each compound showed a broad quantum yield peak in the 450–470 nm region.From the quantum yield and absorption spectra, photolysis spectra were calculated for 5.0 × 10^?5m solutions of each compound. The light-action spectra accurately give the relative rates/μ Einstein that these solutions photolyze at each wavelength. Thus, for example, MeB₁₂ photolyzed faster at pH 7.0 versus pH 1.0 in 510 nm light, but it photolyzed slower at pH 7.0 versus pH 1.0 in 450 nm light. Solutions of each compound photolyzed faster in the ultraviolet region as opposed to the visible (e.g., 310 nm versus 510 nm).Our findings show that the previously reported photolysis rates estimated by others with tungsten lamps provide no valid information about the intrinsic photolability of various alkyl-cobalt bonds. This also applies to the relative white-light photolysis rates reported for the base-on versus the base-off form of MeB₁₂. All such relative rates are artifacts which represent only the extent of overlap between the true action spectrum and the light emission spectrum of an incandescent lamp.