Superconductivity and Mössbauer effect of Nb3Sn produced by Sn implantation

We have implanted Sn, Ge, and Si into Nb films. The resulting Nb-Sn compounds and their annealing behavior have been analyzed by the Mössbauer effect and compared to samples obtained by diffusion of Sn into Nb foils. Mössbauer spectra show that Nb₃Sn is obtained just by implantation, but with a T _cof only 5 K. The 925°C annealing temperature necessary to form the A15 structure with long-range order of Nb chains and T _cvalues up to 17.8 K is at least 100 °C higher in implanted samples than in samples prepared by diffusion of Sn into Nb. This is explained in terms of implantation-induced lattice defects. The metastable A15 phases of Nb₃Ge and Nb₃Si could not be formed by Ge or Si implantation, regardless of target or annealing temperature. It is suggested that the high-energy ions only form phases stable at high temperatures and with low T _cvalues.On leave from North Dakota State University, Fargo, North Dakota.     

The quantity and distribution of radiolabeled dexamethasone delivered to tissue by iontophoresis

A pilot study was conducted in the first of two monkeys using either radiolabeled Dm-Na-P or radiolabeled hydrocortisone sodium succinate, together with lidocaine HCl. This study indicated an approximately tenfold increase in the quantity of Dm-Na-P delivered to the test electrodes (4 mA; 20 minutes) whereas the quantity of hydrocortisone delivered from the test electrodes was only marginally (approximately 10%) increased as compared with that from the controls. In terms of an anti-inflammatory activity, the effective dose of Dm-Na-P in all tissue layers underlying the test electrodes was at least tenfold that of the hydrocortisone. Therefore, further trials with hydrocortisone were abandoned. In the second animal, positive test electrodes (5 mA; 20 minutes, were sited over five joints on the right side of the body and matching control electrodes (0 mA; 20 minutes) were placed over corresponding joints on the left side of the body. The control and test electrodes each contained 1.0 ml tritium-labeled Dm-Na-P (approximately 4.0 mg) and 2.0 ml 4% lidocaine HCl (80 mg). Local tissue concentrations of Dm-Na-P were higher than those that would be obtained by systematic therapy and lower than would be obtained by local injection.     

Renaturation of formyltetrahydrofolate synthetase from urea and guanidinium chloride solutions

Formyltetrahydrofolate synthetase from Clostridium cylindrosporum and Clostridium acidi-urici was denatured in 6 M urea and 4 M guanidinium chloride. Viscometric, fluorimetric and ultracentrifugal measurements were used to determine that the protein is completely unfolded under these conditions. The polypeptide chains refold upon dilution of the denaturant-protein solutions to give final concentrations of 0.5 M urea or 0.1 M guanidinium chloride. In the presence of NH4+, but not in its absence, the refolded proteins associate to produce the catalytically active tetramer. Refolding and reassociation were followed by measuring changes in protein fluorescence and by determination of sedimentation constants. Under most conditions 80% of the enzymic activity is recovered.     

Factors that contribute to the botulinal safety of reduced-fat and fat-free process chesse products

The effects of fat, type of natural cheese, and adjunct process cheese ingredients were evaluated to determine factors that contribute to the botulinal safety of reduced-fat (RF) process cheese products stored at 30 degrees C. In the first set of experiments, pasteurized process cheese products (PPCPs) were formulated using full-fat (FF) Cheddar, 30% RF Cheddar, or skim milk (SM) cheese as cheese-base types and were standardized to 59% moisture, pH 5.75, 2.8 or 3.2% total salts, and 15 to 19% fat. Subsequent trials evaluated the effect of fat levels and adjunct ingredients in PPCPs made with SM, RF, and FF cheese (final fat levels, less than 1, 13, and 24%, respectively). When fat levels of PPCPs were comparable (15.1, 19.1, and 16.2 for product manufactured with SC, RE and FF cheese, respectively), botulinal toxin production was delayed for up to 2 days in PPCPs formulated with SM compared with RF or FF cheese; however, the effect was not statistically significant. When fat levels were reduced to less than 1% in SM PPCPs, toxin production was delayed 2 weeks in products made with SM compared with RF or FF cheese manufactured with 13 or 24% fat, respectively. The antibotulinal effect of adjunct ingredients varied among the products manufactured with different fat levels. Sodium lactate significantly delayed toxin production (P < 0.05) for all fat levels tested, whereas beta-glucan fat replacer did not delay toxin production. An enzyme-modified cheese used as a flavor enhancer significantly delayed toxin production (P < 0.05) in SM (less than 1% fat) products but had little to no inhibitory effect in RF (13% fat) and FF (24% fat) cheese products. Similarly, monolaurin increased the time to detectable toxin in SM products but was ineffective in RF or FF cheese products. These results verify that RF PPCPs exhibit greater safety than FF products and that safety may be enhanced by using certain adjunct ingredients as antimicrobials.     

Antibotulinal activity of process cheese ingredients

Ingredients used in the manufacture of reduced-fat process cheese products were screened for their ability to inhibit growth of Clostridium botulinum serotypes A and B in media. Reinforced clostridial medium (RCM) supplemented with 0, 0.5, 1, 2, 3, 5, or 10% (wt/vol) of various ingredients, including a carbohydrate-based fat replacer, an enzyme-modified cheese (EMC) derived from a Blue cheese, sweet whey, modified whey protein, or whey protein concentrate, did not inhibit botulinal growth and toxin production when stored at 30 degrees C for 1 week. In contrast, RCM supplemented with 10% soy-based flavor enhancer, 10% Parmesan EMC, or 5 or 10% Cheddar EMC inhibited botulinal toxin production in media for at least 6 weeks of storage at 30 degrees C. Subsequent trials revealed that the antibotulinal effect varied significantly among 13 lots of EMC and that the antimicrobial effect was not correlated with the pH or water activity of the EMC.