Ocular biometric measurements in cataract surgery candidates in Portugal

This work was supported by Portuguese research Grant numbers PEst-OE/FIS/UI0068/2011 and UID/FIS/00068/2013 through the FCT-MEC, the "Plurianual" financial contribution of "Fundacao para a Ciencia e Tecnologia", Portugal and Sociedade Portuguesa de Oftalmologia PhD Grant. Fundacao para a Ciencia e a Tecnologia-PEst-OE/FIS/UI0068/2011 and UID/FIS/00068/2013 - Prof Paulo Ribeiro. Sociedade Portuguesa de Oftalmologia-N/A-Dr Tiago Ferreira. Portuguese research Grant numbers PEst-OE/FIS/UI0068/2011 and UID/FIS/00068/2013 through the FCT-MEC, the "Plurianual" financial contribution of "Fundacao para a Ciencia e Tecnologia", Portugal and Sociedade Portuguesa de Oftalmologia PhD Grant. EditorObjective: Describe the ocular biometric parameters and their associations in a population of cataract surgery candidates. Methods: A cross-sectional study of 13,012 eyes of 6,506 patients was performed. Biometric parameters of the eyes were measured by optical low-coherence reflectometry. The axial length (AL), mean keratometry (K) and astigmatism, anterior chamber depth (ACD) (epithelium to lens), lens thickness (LT), and Corneal Diameter (CD) were evaluated. Results: The mean age was 69 ± 10 years (44–99 years). Mean AL, Km, and ACD were 23.87 ± 1.55 mm (19.8–31.92 mm), 43.91 ± 1.71 D (40.61–51.14 D), and 3.25 ± 0.44 mm (2.04–5.28 mm), respectively. The mean LT was 4.32 ± 0.49 mm (2.73–5.77 mm) and the mean CD was 12.02 ± 0.46 mm (10.50–14.15 mm). The mean corneal astigmatism was 1.08 ± 0.84 D (0.00–7.58 D) and 43.5% of eyes had astigmatism ≥ 1.00 D. Male patients had longer AL and ACDs (p <.001) and flatter corneas (p <.001). In regression models considering age, gender, Km, ACD, LT, and CD, a longer AL was associated with being male and having higher ACD, LT and CD. Conclusions: These data represent normative biometric values for the Portuguese population. The greatest predictor of ocular biometrics was gender. There was no significant correlation between age and AL, ACD, or Km. These results may be relevant in the evaluation of refractive error and in the calculation of intraocular lens power. © 2017 Ferreira et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.publishersversionpublishe

Sequence, chromophore extraction and 3-D model of the photoactive yellow protein from Rhodobacter sphaeroides

The photoactive yellow protein (pyp) gene has been isolated from Rhodobacter sphaeroides by probing with a homologous PCR-product. A sequence analysis shows that this pyp gene encodes a 124 AA protein with 48% identity to the three known PYPs. Downstream from pyp, a number of adjacent open reading frames were identified, including a gene encoding a CoA-ligase homologue (pCL). This latter protein is proposed to be involved in PYP chromophore activation, required for attachment to the apoprotein. We have demonstrated the presence of the chromophoric group, previously identified in PYP from Ectothiorhodospira halophila as trans 4-hydroxy cinnamic acid, in phototrophically cultured R. sphaeroides cells by capillary zone electrophoresis. The basic structure of the chromophore binding pocket in PYP has been conserved, as shown by a 3D model of R. sphaeroides PYP, constructed by homology-based molecular modelling. In addition, this model shows that R. sphaeroides PYP contains a characteristic, positively charged patch

Maarten Prak, Catharina Lis, Jan Lucassen en Hugo Soly, Craft guilds in the early modern Low Countries. Work, power, and representation

Photoactive yellow protein (PYP) is a photoreceptor that has been isolated from three halophilic phototrophic purple bacteria. The PYP from Ectothiorhodospira halophila BN9626 is the only member for which the sequence has been reported at the DNA level. Here we describe the cloning and sequencing of the genes encoding the PYPs from E.halophila SL-1 (type strain) and Rhodospirillum salexigens. The latter protein contains, like the E.halophila PYP, the chromophore trans p-coumaric acid, as we show here with high performance capillary zone electrophoresis. Additionally, we present evidence for the presence of a gene encoding a PYP homolog in Rhodobacter sphaeroides, the first genetically well-characterized bacterium in which this photoreceptor has been identified. An ORF downstream of the pyp gene from E.halophila encodes an enzyme, which is proposed to be involved in the biosynthesis of the chromophore of PYP. The pyp gene from E.halophila was used for heterologous overexpression in both Escherichia coli and R.sphaeroides, aimed at the development of a holoPYP overexpression system (an intact PYP, containing the p-coumaric acid chromophore and displaying the 446 nm absorbance band). In both organisms the protein could be detected immunologically, but its yellow color was not observed. Molecular genetic construction of a histidine-tagged version of PYP led to its 2500-fold overproduction in E.coli and simplified purification of the heterologously produced apoprotein. HoloPYP could be reconstituted by the addition of p-coumaric anhydride to the histidine-tagged apoPYP (PYP lacking its chromophore). We propose to call the family of photoactive yellow proteins the xanthopsins, in analogy with the rhodopsins