Research Notes : U.S.S.R. : Subunit composition of glycinin from various samples of cultivated and wild soybean

The major storage protein of llS class of soybean seeds, glycinin, has a complex subunit structure. Each of the six subunits is composed of two pro-tein molecules (acidic and basic), linked via disulphide bonds (Badley et al., 1975). Depending on subunit, the acidic moiety molecular weight varies from 37,000 to 42,000, with one exception (m.w. 10,000)

Laboratory intercomparison of solar absorptance and thermal emittance measurements at room temperature

Solar thermal absorber coatings play an important role in the opto-thermal efficiency of receivers in Concentrated Solar Power (CSP). Two standard figures of merit are the solar absorptance αsol and thermal emittance εth, derived from spectral directional hemispherical reflectance measurements at room temperature. These two figures of merit allow comparing coating formulations in terms of performance and durability. In this study, a black coating and a solar selective coating are optically characterized by different laboratories to compare spectral datasets, solar absorptance αsol and thermal emittance εth calculations. The comparison includes various benchtop spectrophotometers operating in the UV-VIS-NIR and Infrared spectral ranges as well as three commercial portable reflectometers/emissometers. A good agreement is found between the nine parties participating in this intercomparison campaign. The black coating αsol value is 96.6 ± 0.2%, while the solar selective coating αsol value is 94.5 ± 0.4%. For the thermal emittance, spectral data is concatenated and integrated from 0.3 to 16 μm. The black coating εth value calculated at 650 °C is 80.8 ± 3.8%, while the solar selective coating εth value calculated at 650 °C is 25.0 ± 0.5%

Preparation of gelatin microbeads with a narrow size distribution using microchannel emulsification

The purpose of this study was to prepare monodisperse gelatin microcapsules containing an active agent using microchannel (MC) emulsification, a novel technique for preparing water-in-oil (W/O) and oil-in-water (O/W) emulsions. As the first step in applying MC emulsification to the preparation of monodisperse gelatin microcapsules, simple gelatin microbeads were prepared using this technique. A W/O emulsion with a narrow size distribution containing gelatin in the aqueous phase was created as follows. First, the aqueous disperse phase was fed into the continuous phase through the MCs at 40°C (operating pressure: 3.9 kPa). The emulsion droplets had an average particle diameter of 40.7 μm and a relative standard deviation of 5.1%. The temperature of the collected emulsion was reduced and maintained at 25°C overnight. The gelatin microbeads had a smooth surface after overnight gelation; the average particle diameter was calculated to be 31.6 μm, and the relative standard deviation, 7.3%. The temperature was then lowered to 5°C by rapid air cooling and finally dried. The gelatin beads were dried and could be resuspended well in iso-octane. The had an average particle diameter of 15.6 μm, and a relative standard deviation of 5.9%. Using MC emulsification, we were able to prepare gelatin microbeads with a narrow size distribution. Since this emulsification technique requires only a low-energy input, it may create desirable experimental conditions for microencapsulation of unstable substances such as peptides and proteins. This method is promising for making monodisperse microbeads

Goniometer-based femtosecond crystallography with X-ray free electron lasers

The emerging method of femtosecond crystallography (FX) may extend the diffraction resolution accessible from small radiation-sensitive crystals and provides a means to determine catalytically accurate structures of acutely radiation-sensitive metalloenzymes. Automated goniometer-based instrumentation developed for use at the Linac Coherent Light Source enabled efficient and flexible FX experiments to be performed on a variety of sample types. In the case of rod-shaped Cpl hydrogenase crystals, only five crystals and about 30 min of beam time were used to obtain the 125 still diffraction patterns used to produce a 1.6-Å resolution electron density map. For smaller crystals, high-density grids were used to increase sample throughput; 930 myoglobin crystals mounted at random orientation inside 32 grids were exposed, demonstrating the utility of this approach. Screening results from cryocooled crystals of β2-adrenoreceptor and an RNA polymerase II complex indicate the potential to extend the diffraction resolution obtainable from very radiation-sensitive samples beyond that possible with undulator-based synchrotron sources