Unique rearrangement of ergocalciferol side chain in vitro: production of a biologically highly active homologue of 1,25-dihydroxyvitamin D3

In vitro incubation of 24-epi-25-hydroxyvitamin D2 with chicken kidney homogenate produced several compounds, one of which had an affinity equal to that of 1,25-dihydroxyvitamin D2 for the chick intestinal receptor. The affinity of 24-epi-1,25-dihydroxyvitamin D2 for the same receptor was found to be half that of 1,25-dihydroxyvitamin D2. The unknown compound was produced only when homogenate was prepared from pooled kidneys taken from both vitamin D deficient and replete chickens. The compound has been tentatively identified as 1,25-dihydroxy-22-dehydro-26-homovitamin D3 by ultraviolet absorption spectrophotometry and mass spectrometry. Chemical synthesis of 1,25-dihydroxy-22-dehydro-26-homovitamin D3 provided additional evidence for the structure. Administration of this 26-homologue of 1,25-dihydroxyvitamin D3 at the dose level of 650 pmol/rat stimulated bone calcium mobilization in the hypocalcemic rat equal to that of 1,25-dihydroxyvitamin D3. Thus, this paper demonstrates unique methyl migration on the side chain of 24-epi-1,25-dihydroxyvitamin D3 to form a more biologically potent analogue.     

Inhibition of virus multiplication by immunoactive peptides

In the present study we show that peritoneal macrophages obtained from the mice treated with the immunoactive peptides inhibit the multiplication of Herpes simplex virus type 1 (HSV-1) and type 2 (HSV-2), but not that of vesicular stomatitis virus (VSV), and that the intraperitoneal administration of the peptides suppresses the infection with HSV-1 in mice.     

Modeling of experiments on biofilm penetration effects in a fluidized bed nitrification reactor

A four-component, diffusion-reaction model with double Michaelis-Menten kinetics was used to describe the experimental data obtained from a laboratory biofilm, fluidized-bed nitrification reactor. Theory and experiment demonstrated that the stoichiometric ratio (3.5 mg O(2)/mg NH(4) (+)-N) can be employed as a criterion to determine whether the limiting substrate is oxygen or ammonia. For the present work, in the range of concentrations where limitation occurred, 4 mg/L NH(4) (+)-N and 14 mg/L O(2), the ratio of oxygen to ammonia in the bulk liquid determined which substrate was penetration-limiting-O(2) if <3.5 and NH(4) (+) if > 3.5. Halforder kinetics with respect to the limiting substrate described the apparent overall rates. Simulations provided biofilm concentration profiles which demonstrated the role of the oxygen-ammonia ratio. Experiments indicated that, generally, high NO(2) (-) concentrations can be expected. These depend on the residence time, biofilm area, and oxygen concentration. This dependency was investigated with the model, as was the parametric sensitivity with respect to the saturation constants. Particularly important for the NO(2) (-) levels were the ratios of the saturation constants for oxygen.     

Immunoreactive glucagon in the vascular walls of the rat

We detected immunohistochemically immunoreactive glucagon (IRG) in the smooth muscle of blood vessels and the myoepithelial cell of sweat glands of rats using two antisera against pancreatic glucagon; OAL-123 and 30K. The content of IRG in the blood vessels was found to be 320-1, 270 pg per g wet tissue weight. Filtration of the extracted IRG through a Bio Gel P-30 column yielded a single peak of IRG at 3,500 daltons, the same elution volume of pancreatic glucagon. These findings suggest that the blood vessels of the rats is one of the extrapancreatic sources of IRG in plasma, although physiological role of the IRG is not known.