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P Bloebaum

Publications and source records attributed to P Bloebaum.

4 recordsLinked to original sources

Bioaerosol sampling in field studies: can samples be express mailed?

Bioaerosol sampling for viable microorganisms was conducted in 25 dairy barns in summer and in winter to examine the relationship of sample storage and shipping in determining bioaerosol concentrations separately for yeasts, molds, mesophilic bacteria, and thermophilic organisms. The study also compared the performance of three sampling methods--(1) all-glass impinger (AGI) used with peptone solution in both seasons and (2) betaine solution in winter; and (3) the nuclepore filtration and elution (NFE) method, using air filtration with subsequent elution and culturing--which were studied in a pairwise fashion with duplicate, simultaneous, side-by-side sampling. For each sample, one duplicate was analyzed within two hours in a laboratory less than 50 km from the sampling site, while the other was express-mailed to the authors' laboratory. Concentrations of all microorganisms measured by the AGI peptone method were unaffected by mailing in winter, but mesophilic bacteria increased in summer. AGI betaine samples were unchanged except for increased concentrations of molds after mailing in winter. Yeasts and mesophilic bacteria significantly decreased after mailing of NFE samples. Pairwise comparison of the sampling methods in winter yielded no significant differences in airborne concentrations for the yeasts, mesophilic bacteria, and thermophilic bacteria. Both AGI betaine and NFE methods had significantly greater concentrations of molds than AGI peptone. In summer, concentrations of yeasts and mesophilic bacteria were significantly greater with AGI peptone, as were molds with the NFE method.(ABSTRACT TRUNCATED AT 250 WORDS)

Air Pollutants, Occupational↗

Commercial levels of chymosin production by Aspergillus.

We have increased the production of bovine chymosin in Aspergillus niger var. awamori to more than one gram per liter of secreted authentic enzyme by combining a mutagenesis protocol with a novel robotic screening program. Analysis of the superior chymosin producing strains indicated that they have enhanced capabilities to secrete extracellular proteins.

Aspergillus niger↗

The CaATPase activity of rat-incisor odontoblast vesicles.

An homogenate of rat incisor odontoblasts had Ca2+ and Mg2+ ATPase activity and suitable storage conditions kept it stable for several days. Over 90 per cent of the activity was retained in a vesicle-rich microsomal fraction that removed about 85 per cent of the total material from the homogenate. This fraction was further characterized: the resolved Ca2+-activated ATPase activity, above the basal MgATPase activity, was 0.30 mumol Pi/min-mg total protein, and 50 per cent activated at free [Ca2+] equal 0.8 microM. This calcium dependency is consistent with an intracellular Ca2+-regulated enzymatic activity. The calcium ionophore, A23187, had no measurable effect on the CaATPase activity, which suggests that the odontoblast vesicles do not concentrate Ca2+ in a lipid bilayer compartment. Direct measurement of the uptake of 45Ca2+ by the filtration method and parallel measurements of CaATPase activity on the same preparations under identical conditions indicated that the odontoblast-derived vesicles have a coupling ratio of 0.024 Ca2+/ATP. This low coupling ratio and the lack of detectable compartmentalization of calcium indicate that the CaATPase activity of the odontoblast microsomes is not associated with a calcium pump. The [Ca2+] dependence of the activity suggests the CaATPase is under intracellular Ca2+ control, but its function is unknown.

Animals↗

Sarcoplasmic reticulum interacts with the Ca(2+) indicator precursor fura-2-am.

Fura-2-am, the pentaester precursor of the fluorescent Ca(2+) indicator fura-2, is modified when it is exposed to isolated skeletal muscle sarcoplasmic reticulum vesicles. The modified fura-2-am has enhanced fluorescence, is not sensitive to Ca(2+), and is partially bound to the SR membrane. The isolated product is further converted into fura-2 by esterase. It is suggested that the SR-induced modification is a selective enzymatic hydrolysis of only some of the five ester moieties on fura-2-am. A structure is proposed to account for the results. The potential for this effect of SR on fura-2-am to cause complications in measurements of in vivo intracellular free [Ca(2+)] is noted.

Animals↗