22 research outputs found
The Microbial Communities in Male First Catch Urine Are Highly Similar to Those in Paired Urethral Swab Specimens
Urine is the CDC-recommended specimen for STI testing. It was unknown if the
bacterial communities (microbiomes) in urine reflected those in the distal male
urethra. We compared microbiomes of 32 paired urine and urethral swab specimens
obtained from adult men attending an STD clinic, by 16S rRNA PCR and deep
pyrosequencing. Microbiomes of urine and swabs were remarkably similar,
regardless of STI status of the subjects. Thus, urine can be used to
characterize urethral microbiomes when swabs are undesirable, such as in
population-based studies of the urethral microbiome or where multiple sampling
of participants is required
Technically successful ultrasound-guided percutaneous sural nerve needle biopsy in a patient with indeterminate peripheral neuropathy
Characterisation of three ACC synthase gene family members during post-harvest-induced senescence in broccoli (Brassica oleracea L. var. italica)
We investigated the gene expression profiles of different members of the 1-aminocyclopropane-1-carboxilic acid (ACC) synthase (EC 4.4.1.14) gene family in broccoli (Brassica oleracea L. var. italica) during the post-harvest-induced senescence process. Using RT-PCR, three different cDNAs coding for ACC synthase (BROCACS1, BROCACS2 and BROCACS3) were amplified from floret tissue at the start of the senescence process. The three genes share relatively little homology, but have highly homologous sequences in Arabidopsis thaliana, and could be functionally related to these counterparts. Southern analyses suggest that BROCACS1 and BROCACS3 are present as single copy genes, while there are probably two copies of BROCACS2. All three genes showed different expression patterns: BROCACS1 is likely to be either wound - or mechanical stress-induced showing high transcript levels after harvesting, but no detectable expression afterwards. BROCACS2 shows steady expression throughout senescence, increasing at the latest stages, and BROCACS3 is almost undetectable until the final stages. Our results suggest that BROCACS1 could be required to initiate the senescence process, while BROCACS2 would be the main ACC synthase gene involved throughout the post-harvest-induced senescence. BROCACS3's expression pattern indicates that it is not directly involved in the initial stages of senescence, but in the final remobilization of cellular resources
Standard inocula preparations reduce the bacterial diversity and reliability of regulatory biodegradation tests
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Effect of arginine on the aggregation of protein in freeze-dried Formulations containing sugars and polyol: 1-formulation development
L-arginine was introduced into protein-based freeze-dried formulations to study the ability of arginine to reduce/prevent from protein aggregation during manufacturing, storage and reconstitution of lyophilized protein-based pharmaceuticals. As L-arginine is known to be very hygroscopic, additional excipients which could provide a moisture buffering capacity need to be introduced into the formulation. In the first part of our study-excipient formulation development-the screening of a number of sugars/polyols has been done in order to select the best combination of excipients that, in a complex with L-arginine, can (i) produce freeze-dried cakes with elegant appearance, adequate mechanical properties and reconstitution times, and (ii) resist/minimise the moisture sorption. Various freeze-dried cakes containing L-arginine in combination with mannitol, trehalose, lactose and sucrose were produced and analysed by TGA, DSC, texture analysis, moisture sorption, cake shrinkage, TVIM and SEM. The non-linear dependencies of the physicochemical properties of the freeze-dried cakes on the sugar-to-mannitol ratios were found. The best combinations of excipients (L-arginine, mannitol and trehalose) were selected to be used in the second part of this work, in which the impact of each selected formulation will be studied in relation to the aggregation of a protein
