This sacrificial layer approach allows for high pattern fidelity and stability, and it leads directly to stable, micrometer-thick, and contamination-free TNP patterns for developing the SS-DSSC array for miniature high-voltage applications. Methods Fabrication of TNP patterns In preparing photoanodes connected in https://www.selleckchem.com/products/ly3023414.html series for a high-voltage VS-4718 concentration DSSC array, micropatterns of

the TNP were constructed on a pre-patterned fluorine-doped tin oxide (FTO) glass. An array of 20 FTO electrodes, where each electrode has a width of 500 μm and a gap of 500 μm between two adjacent electrodes, was prepared using photolithography and a dry etching process. A glass substrate with pre-patterned FTO was cleaned with acetone, deionized water, and ethanol in sequence and dried with nitrogen flow. The cleaned substrate was then dried at 90°C in a vacuum oven for 10 min to remove any residual water and subsequently treated with ultraviolet Autophagy signaling inhibitor ozone for 5 min. In order to improve the adhesion and the mechanical strength of the TNP layer [13], the treated FTO glass was soaked in an aqueous solution of 40 mM TiCl4 at 70°C for 30 min. The FTO glass was then cleaned in the same way described above. Figure  1 shows the schematic diagram illustrating the fabrication

of a patterned TNP layer on the FTO glass. The entire fabrication processes of patterning TNP are as follows: An elastomer stamp with patterns, complementary to desired TNP patterns, was made of poly-(dimethylsiloxane) (PDMS). For fabricating complementary patterns of a sacrificial Loperamide layer (SL) on the FTO glass, a fluorous polymer (3 M Novec™ EGC-1700, 3 M Novec, Manassas, VA, USA) dissolved in a highly fluorous solvent (3 M Novec™ HFE-7100) was dip-coated on the prepared PDMS stamp. Figure  1a shows the transfer printing process of the complementary patterns of the SL on the PDMS stamp onto the FTO glass. Note that no

additional pressure or heat is required during transfer printing due to the lower surface energy of the PDMS stamp than that of the FTO glass [14]. Ti-Nanoxide T (Solaronix SA, Aubonne, VD, Switzerland) paste was subsequently prepared on the SL-patterned FTO glass to form a TNP layer using a doctor-blading technique, as shown in Figure  1b. The TNP film was soft-cured at 50°C for 3 min for the fixation of the TNPs to ensure stability during the following lift-off process. In the soft-cure treatment, the duration of heating plays a critical role in patterning the TNP layer of a few micrometers thick; the TNP layer should be sufficiently soft for the application of the lift-off process but structurally strong enough to prevent the collapse of the TNP stacks during the lift-off process.

We also found these associations between bacteriocin production and ExPEC virulence determinants among human fecal E. coli isolates. Moreover, we have found new associations between 3 bacteriocin types (microcin B17, colicins Ia and S4) and the ExPEC virulence characteristics of human fecal E. coli strains. Given that colicin Ia and microcin B17 are known to be encoded on relatively large plasmids, it is possible that the association with more virulent strains is due to other genes being harbored on these plasmids, and not by colicin synthesis itself. However, colicin S4 was found to be encoded on a small plasmid (7.4 kb) [40] that was similar to the colicin E1-encoding plasmid

(6 kb) [21]. Since these small plasmids do not encode virulence factors, colicin S4 appears to be a potentially important virulence factor and/or an important factor of resident E. coli strains. The presence of virulence Selleck ZD1839 determinants (e.g. genes encoding P-fimbriae, siderophore aerobactin, hemolysin and expression of O antigens, which are typical for ExPEC strains; and capsular types K1 and

K5) are associated with resident E. coli strains [41–44]. At the same time, ExPEC strains causing extraintestinal infections like urinary tract infections and sepsis/meningitidis are believed to originate from the gut microflora. Their virulence determinants including adhesins (P-fimbriae, S-fimbriae), toxins (e.g. hemolysin, cytotoxic necrotizing factor) and siderophores (e.g. aerobactin) appear to be important for E. coli strains this website to survive in the extraintestinal environment [45–47]. On the other hand, we found that diarrhea-associated strains from our set of 1181 selleck kinase inhibitor fecal E. coli had a lower prevalence of bacteriocinogeny and a lower frequency of several bacteriocin producers. In addition, no specific bacteriocin types appear to be associated with virulence determinants that are typical for these strains. Unlike fecal strains which have the characteristics of ExPEC strains, diarrhea-associated strains are not considered to be resident human E. coli strains, which may explain

the lower prevalence of bacteriocin genes. In summary, bacteriocin synthesis is linked to strains with ExPEC characteristics and appears to increase the ability of E. coli to reside in the human gut. Moreover, at least several bacteriocin-encoding genes should be also considered as factors which increase the virulence of ExPEC strains. Conclusions The frequency of bacteriocin-encoding genes was found to be positively correlated with the frequency of E. coli virulence determinants. E. coli with virulence characteristics of ExPEC strains, i.e. strains encoding virulence factors S-fimbriae (sfa), P-fimbriae (pap), cytotoxic necrosis factor (cnf1), α-hemolysin (α-hly) and aerobactin biosynthesis (aer, iucC) were more often found to harbor genes encoding synthesis of microcins (H47, M, V and B17) and colicins (E1, Ia and S4) than other selleck products tested E. coli strains.

In contrast, expression of Seliciclib supplier hsa-miR-337-3p was only detected in three gastric cancer cell lines, i.e., SNU-5, HGC27, and SGC-7901, at a low level (Figure 2B). Figure 2 Expression of hsa-miR-134 and hsa-miR-337-3p in the nonmalignant gastric cell line GES and nine gastric

cancer cell lines. A, hsa-miR-134; B, hsa-miR-337-3p. Effect of mimics and inhibitors of hsa-miR-134 and hsa-miR-337-3p on MKN-45 cell proliferation To determine the effects of hsa-miR-134 and hsa-miR-337-3p on the regulation of gastric cancer growth and invasion, we selected the MKN-45 cell line according to its expression levels of these two miRNAs. The mimic was used to determine whether overexpression find more of these two miRNAs could inhibit tumor cell invasion in vitro, whereas inhibitors were used as controls. (Although they were downregulated in gastric tumor cells, they may have certain levels of expression in tumor cells, and inhibition of their expression may selleck chemicals also promote tumor cell invasion.) We transfected hsa-miR-134 or hsa-miR-337-3p mimics or inhibitors into MKN-45 cells and performed a cell viability assay. The data revealed that the changed expression of hsa-miR-134 or hsa-miR-337-3p only slightly affected MKN-45 cell proliferation (Figure 3). miRNA mimics and inhibitors used in this study were listed in Additional file 3: Table S2. Figure 3 Time-course effects of miRNAs on the regulation

of gastric cancer MKN-45 cell proliferation. Endonuclease A, hsa-miR-337-3p mimic-transfected MKN-45 cells. B, hsa-miR-134 inhibitor-transfected MKN-45 cells. Data are expressed as mean ± SD; n=4. Expression of hsa-miR-337-3p affects MKN-45 cell migration and invasion Since these miRNAs were differentially expressed in primary and secondary gastric cancer tissues, we investigated the effects of hsa-miR-134 and hsa-miR-337-3p on

the regulation of gastric cancer cell migration by transfecting hsa-miR-134 and hsa-miR-337-3p mimics or inhibitors into MKN-45 cells and then measured the tumor cell migration capacity. Next, the capacity of the transfected cells was examined using a Transwell-Matrigel invasion assay. Our data showed that transfection with the hsa-miR-134 mimic or inhibitor in MKN-45 cells did not affect the tumor cell invasion capacity (Figure 4A; P>0.05). In contrast, the hsa-miR-337-3p mimic significantly decreased the number of invaded cells (Figure 4B; P<0.05), indicating that hsa-miR-337-3p overexpression may decrease the invasive ability of gastric cancer cells. Figure 4 The effect of hsa-miR-337-3p or hsa-miR-134 mimics or inhibitors on the regulation of gastric cancer cell invasive capacity. A, The migrated cell number of the hsa-miR-134 inhibitor-transfected MNK-45 cells; B: The migrated cell number of the hsa-miR-337-3p mimic-transfected MNK-45 cells. Data are expressed as mean ± SD; n=4; *P<0.05, as compared to the control oligonucleotide (NC) treated group.

However, when small fragments closer to the jamA ORF start site were used, OICR-9429 supplier the promoter activity increased significantly, with maximal activity observed for the fragment -76 – 0 bp upstream of jamA. The promoter in the -76 – 0 region appeared to require the sequence fragment -38 – 0, as another

construct containing the region upjamA-96 – -38 did not have any promoter activity. The entire 269 bp upjamI upstream region also displayed strong promoter activity relative to the positive control. Promoter activity was lost using fragments encompassing -269 – -68 bp, but restored using the fragment -67 – 0 bp (Figure 5). Inspection of the sequences included in these active, truncated regions of upjamA and upjamI led to the identification of possible conserved promoter elements in close proximity to the ORF start sites for both genes (Table 1). Figure 5 Activity of truncated up jamA and up jamI regions in the β-galactosidase assay. Trimmed regions are represented by blue shaded figures with associated base pair numbers. Red arrows indicate the start codon of the downstream ORF (jamA or jamI). Relative activity was calculated on same scale as Figure 4. Standard error is represented by error bars. To quantitatively Target Selective Inhibitor Library determine the promoter activities of the DNA fragments, a series of β-galactosidase assays incorporating a serial dilution of E. coli soluble selleck chemicals protein lysate was also used in order to avoid saturation problems in color development (Figure

6). These data were used to calculate β-galactosidase activity in terms of nmol ONPG hydrolyzed min-1 mg soluble protein-1 for each of the upstream fragments with any detectable promoter activity. The strongest promoter was the section Dimethyl sulfoxide upstream of the jamaicamide TSS (-902 – -832 upstream of jamA), with an average of approximately 950 nmol ONPG hydrolyzed min-1 mg soluble protein-1. The promoter immediately upstream of jamA (-76 – 0) and those upstream of jamB, jamD, and jamI yielded lower values, with upjamA,

upjamB and upjamI between 500-700 nmol ONPG hydrolyzed min-1 mg soluble protein-1, and upjamD at approximately 265 nmol ONPG hydrolyzed min-1 mg soluble protein-1. Reduced activity was found for promoters upstream of jamC, jamG, and jamN, with values ranging from approximately 75 to 150 nmol ONPG hydrolyzed min-1 mg soluble protein-1. The arabinose promoter positive control construct yielded an average value of 170 nmol ONPG hydrolyzed min-1 mg soluble protein-1. Figure 6 Specific activity of the strongest promoters in the β-galactosidase assay. Base pair number relative to gene ORF start site is provided when necessary. Standard error is represented by error bars. Isolation and characterization of possible transcription factors from a pulldown assay To determine whether jamaicamide regulatory proteins are encoded in the L. majuscula JHB genome, we performed DNA – protein “”pulldown”" experiments to isolate proteins with affinity to the upstream region of jamA.

This once again favors the hypothesis that sigF is not strongly auto-regulated. Figure 4 Role of CC3252 on expression of CC2906, CC3255 and sigF genes . Results shown are from qRT-PCR performed with total RNA extracted from exponential growth phase cells under control conditions (no stress) or stressed with potassium dichromate (K2Cr2O7). We analyzed the parental strain NA1000 without expression plasmid pJS14, NA1000 with the empty plasmid pJS14 and NA1000 with pJS14 containing CC3252 gene (CC3252++). Values represent the fold increase

of CC2906, CC3255 and CC3253 (sigF) expression in the corresponding strain, exposed or not to the stress condition, compared with the parental strain NA1000 without pJS14 growing under control conditions. Results were normalized using gene CC0088 as the endogenous control, which was constitutively expressed check details in the

samples analyzed. Data are mean values of two independent experiments; bars represent the standard error. Statistical analysis is shown in Additional file 1: Table S4. A further attempt to investigate the role of nrsF as a possible negative regulator of σF function was carried out by click here trying to construct a null mutant strain in gene nrsF. However, it was not possible to construct a mutant strain by deleting nrsF in the parental strain (data not shown). On the other hand, nrsF could be deleted in the absence of a functional copy of sigF (data not shown), suggesting that high σF activity is apparently responsible for the failure of disrupting nrsF in cells with functional sigF. The putative protein encoded by nrsF is composed of six putative transmembrane segments separated by five short linkers (6 to 19 amino acid residues) and an N-terminal segment of 25 residues (Figure 5B). Alignment of the deduced amino acid sequence of CC3252 with its orthologs from other bacteria (Cupriavidus metallidurans,

Pseudomonas entomophila, Pseudomonas putida, Rhizobium leguminosarum, Maricaulis maris and Sinorhizobium meliloti) revealed two highly conserved cysteine residues (Figure 5A). The cysteine residues of the Caulobacter protein (positions 131 and 181) are probably directed into the periplasmic 4��8C space (Figure 5B), which favors their putative role in the signal transduction process leading to the liberation of σF from NrsF inhibition. Substitution of the conserved www.selleckchem.com/products/Temsirolimus.html cysteines by serine led to two single mutants (SG22, C131S; SG23, C181S) and a double mutant (SG24, C131S-C181S). Even under unstressed conditions, all σF-regulated genes analyzed in qRT-PCR experiments, including sigF and CC3252, were up-regulated in the single mutant strains when compared to the parental strain (Figure 5C). The substitution of both cysteines by serine in NrsF resulted in the highest expression levels of the genes analyzed (Figure 5C).

Five pigs free of A. pleuropneumoniae were inoculated intratracheally at dose of 1.0 × 107CFU/pig

in PBS to prepare the convalescent sera, and three pigs survived. Twenty days after the first infection, the survivors were rechallenged with another identical dose of JL03. Sera were collected a week after the second inoculation and evaluated. Antibody titer of mixed sera from survivors 1:512 was Momelotinib datasheet measured by IHA kit (Lanzhou Bioproducts Factory, Lanzhou, China). Sera were collected before inoculation as control sera. All animals were housed and maintained in isolation facilities in accordance with the Animal Care and Use Committee guidelines of Huazhong Agricultural University. 2-DE and immunoblotting analysis IEF was performed with the IPGphor II™ system (GE Healthcare, USA) and the Immobiline DryStrip™ IPGstrips of 13 cm

(linear 3–10 pH gradient) according to Gorg et al[54]. The prepared ECPs and OMPs (150 μg/strip) was mixed with rehydration buffer (7 M urea, 2 M thiourea, 2% w/v CHAPS, 1%w/v DTT, 0.5%v/v IPG buffer, 0.002% w/v bromophenol blue). The ECPs and OMPs samples were focused for 50 kVh and 75 kVh respectively. After IEF, three gels were run as follows. The IPGstrips were respectively equilibrated for 15 min with 10 mg/ml DTT and 40 mg/ml iodoacetamide in equilibration Fedratinib nmr buffer (6 M urea, 2% w/v SDS, 30% v/v glycerol, 0.002% w/v bromophenol blue, 50 mM Tris-HCl, pH 8.8). After equilibration, the second dimension electrophoresis was performed on a 10% SDS polyacrylamide gel using Hoefer SE600 Ruby (Amersham Biosciences). Proteins of one gel were visualized by staining with silver nitrate (Bio Basic Inc). And gel evaluation and data analysis were carried out

using the ImageMaster v 6.01 program (GE Healthcare, USA). Immunoblot was performed according to Mansfield [55]. Gels were blotted onto PVDF transfer membranes (Hybond-P, 0.45 mm; Amersham Biosciences). The membranes were blocked in 5% BSA in TBS +0.05%(v/v) Tween 20 for 1 h at room temperature and probed with the convalescent swine sera and control sera (1:1000), for 1 h at room temperature, and then were washed and incubated with goat anti-porcine IgG (H+L) -HRP (1:5,000) GPX6 (Southern Biotech, Birmingham, AL, USA) for 1 h at room temperature, followed by development with Supersignal west pico chemiluminescent substrate (Pierce, Rockford, IL, USA) and imaged on the Image Station 2000 MM (Kodak, Rochester, NY, USA). All experiments were done in triplicate. In-gel digestion of proteins[5] Protein spots of interest were excised from gels and Vorinostat solubility dmso detained with 100 μl 30 mM potassium ferricyanide and 100 μl 100 mM sodium thiosulfate (at a ratio of 1:1). And the gel pieces were shrunken with 50 μl acetonitrile and then re-swollen with 5 μl of 25 mM ammonium bicarbonate containing 10 ng of trypsin at 4°C for 30 min. In-gel tryptic degradation was performed overnight at 37°C, followed by three subsequent extractions.

San Clemente, CA. FIK, JH, and AW served as scientific consultants for StemTech International. Authors’ contributions

CAR, JH, FIK, and AW contributed to the study conception and design, SDR and JM screened the subjects and provided medical oversight, CAR, JYW acquired the data, JP performed the data analysis, CAR, JH, FIK, and AW interpreted the data; All authors were involved in drafting the manuscript and have given final approval of the published version.”
“Introduction Alkalizing agents have been used in high performance sports as a strategy to postpone the SYN-117 mw onset of fatigue during high intensity exercise by slowing the decline in muscle and blood pH [1, 2]. Studies have confirmed that increasing the extracellular pH, via an alkalizer, promotes the

efflux of lactate mTOR inhibitor and H+ from the active muscles [1, 3–5]. Therefore, artificially inducing alkalosis prior to anaerobic exercise may reduce intracellular acidosis and increase the time to fatigue [6, 7] The process known as “bicarbonate loading”, in which sodium bicarbonate is ingested pre-performance, is a popular method of blood alkalization among athletes [6, 8]. According to a recent meta-analysis by Carr et al. [8], sodium bicarbonate enhances performance by 1.7% (±2.0%) for a 60 sec maximal effort, with a dose of 0.3 g kg-1 of body mass being the optimal dose. However, the gastrointestinal (GI) acceptance profile of sodium bicarbonate ADP ribosylation factor is narrow and 10% of humans cannot adequately tolerate the doses needed to elicit an ergogenic effect [6, 9].

Thus, ingesting sodium bicarbonate in high enough doses to induce an adequate modification of the acid–base balance during exercise can be detrimental to performance [6, 9, 10]. Sodium citrate (Na-CIT) is another alkalizing agent that has been studied in sports over a broad array of doses, times and distances but the results on its ergogenic effect have been inconclusive [2–4, 10–14]. Indeed, the meta-analysis by Carr et al. [8] reported an unclear effect on performance (0.0 ± 1.3%) for a 60 sec maximal effort, with a dose of 0.5 g kg-1. Due to this uncertainty, in combination with its lower commercial availability, STI571 mouse Na-CIT has not been used as an alternative to sodium bicarbonate although it has a higher GI tolerance [2, 5, 6]. Na-CIT can enter the sarcolemma through a recently discovered plasma membrane citrate transporter [15], providing new evidence to support its potential effect on performance. Competitive swimming is an ideal model for studying the effectiveness of alkalizing agents due to its high reliance on anaerobic metabolism. Events range in duration from 22 sec (50 m freestyle) to 15 min (1500 m freestyle) with the highest blood lactate concentrations found in the 200 m (~2 min) events. Typical post-race blood lactate concentrations for these events are 6.4, 9.1, and 14.

005). Fluorescent staining (FITC) for chlamydial antigens supported an impairment

of chlamydial growth and inclusion body expansion after 405 nm exposure (Figure 2D-F, 20 J/cm2) compared to C. trachomatis infected cells alone (Figure 2A-C). We also analyzed the effect of irradiation application time post-infection to determine if it was growth phase specific. At 24 h post-infection, irradiation with 405 nm (20 J/cm2) LEDs still demonstrated a significant growth MK5108 chemical structure inhibition (Figure 1B, P < 0.005). C. trachomatis-infected cells treated with red 670 nm LEDs at similar energy densities (5-20 J/cm2) showed no significant effect on growth (data not shown). Figure 1 Effects of 405 nm irradiance on chlamydial growth in HeLa cells. Sotrastaurin supplier (A) HeLa cells were infected with C. trachomatis serovar E at a MOI of 5. (B) Infected cells were then exposed to varying doses of 405 nm at a range of energy densities (5-20 J/cm2) either promptly after infection or 24 h post-infection (24 h Poziotinib supplier post). Treatments are grouped based on post-hoc comparisons for convenience. The effect of 405 nm on chlamydial growth was assessed during active and persistent stages induced with penicillin (B and C). Growth was determined using quantitative real-time PCR to determine the ratio of chlamydial and eukaryotic housekeeping genes (16S:

GAPDH respectively) 48 h post-infection on cDNA reverse transcribed from RNA. Mean ± standard deviation are plotted for the two replicated experiments. Statistical significance was determined post-hoc using a Bonferonni adjustment comparing all groups against C. trachomatis-infected HeLa cells alone (CTE); * P < 0.05, ** P < 0.005. Figure 2 Anti-chlamydial properties of 405 nm irradiance. (A-C) HeLa cells were infected with C. trachomatis serovar E at a MOI of 5 without exposure to Bortezomib chemical structure photodiodes. (D-F) Infected cells were exposed to 405 nm LEDs at 20 J/cm2 promptly after infection to evaluate anti-chlamydial effects during an acute chlamydial infection. Cells were fixed and stained with dapi (blue) (B and E) and anti-chlamydial (green) (C and F) antibody 48 hours post-infection. Bar = 10μm. Considering many chronic chlamydial infections are

in a persistent stage of growth, we tested the effect of 405 nm on chlamydial growth after penicillin-induced persistence. As shown in Figure 1C, 405 nm retarded chlamydial growth during a persistent state (P < 0.05) at 20 J/cm2, though the result was not as pronounced as it was in the active state. Once again, no effect was seen with 670 nm treatment (data not shown). The effect of 405 nm irradiation on IL-6 production in C. trachomatis-infected HeLa cells Previous studies have identified IL-6 as a pro-inflammatory cytokine associated with immunopathologic effects in chronic C. trachomatis infections [12, 13]. In this study, we demonstrated elevated IL-6 levels post-chlamydial infection compared to uninfected cells (Figure 3A, P < 0.005). C.

[17, 18]. According to this, the incidence of these infections is rising because of an increase in the number of immunocompromised patients, diabetes, cancer, alcoholism, vascular insufficiencies BAY 80-6946 cost and organ transplants. VEGFR inhibitor Almost half of these infections are idiopathic, because we are not able to identify any underlying lesion at the site of the NSTI [7]. The best examples of such cases are scrotal

or penile NF. Causative organisms are numerous and often may be polymicrobial (Table 3) [18, 19]. There is no age or sex predilection for infection [18]. Because of the accompanying systemic illness and profound tissue inflammation, these patients are usually critically Hormones inhibitor ill and have prolonged ICU stay. They need critical care therapy and complex surgical management, and can be treated in a specialized facility such as a burn center or a burn unit [7]. Laboratory based scoring systems as LRINEC score test (The Laboratory Risk Indicator for Necrotizing Fasciitis) [20] (Table 3.) or APACHE II score test (The Acute Physiology and Chronic Health Evaluation) may help in the early diagnosis of NF [21]. Both scoring tests are not NSTI specific, but are accurate predictors of mortality rates

in most NF cases. Pathophysiology and microbiological findings According to the updated consensus for NSTIs (1,2), microbial invasion of skin and

subcutaneous tissue occurs either through external trauma and surgical wounds, or directly through bacterial invasion from a perforated viscus. Table 4 present potential antibiotic therapeutic regimens GNA12 for certain pathogenic organisms and predisposing factors. Microorganisms appearing in the skin and subcutaneous tissue spaces produce various endo- and exotoxins that cause prolonged vasoconstriction in the dermal capillary network. When these toxins are released into the systemic circulation, they produce the SIRS, which can progress into septic shock, MODS and finally, death [1, 2, 14]. The central pathohistological point in the pathogenesis of NSTIs is the thrombosis of perforating vessels of the skin and subcutis [17]. As the spread and extent of infection do not correspond with overlying skin changes, an inexperienced surgeon might not clearly determine the seriousness and extent of infection that takes place under the skin surfaces and in the subcutaneous space. In case of fulminating NF, MODS will develop within the first 24 hours of infection. In this case the disease will very often become fatal if not promptly recognized and treated with extensive surgical debridement, appropriate a combination of the antibiotics, and intensive care resuscitation [21].

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New York, pp. 221–255 Hirsch RE (2003) Hemoglobin fluorescence. In: Nagel RL (ed) Methods in NADPH-cytochrome-c2 reductase hemoglobin disorders. Series in molecular medicine. Humana Press, New Jersey, pp 133–154 Hirsch RE, Brody SS (1978) Spectral properties of chlorophyll-a monolayers in the presence of an exogenous electron donor and acceptor. Eur J Biochem 89:281–286CrossRefPubMed Hirsch RE, Brody SS (1979) Spectral properties of chlorophyll a monolayers: monolayers of chlorophyll a and pheophytin at a gas–water interface. Photochem Photobiol 29:589–596CrossRef Hirsch RE, Brody SS (1980) Absorption spectra of mixed monomolecular films of chlorophyll and photosynthetic electron carriers at a gas–water interface. Arch Biochem Biophys l99:506–5l4 Hirsch RE, Nagel RL (1981) Conformational studies of hemoglobins using intrinsic fluorescence measurements.