Table 2 Primers used in this study Primer Sequence (5′-3′) JAF 401 # GAG GAA TAA TAA ATG CTG ATT CTG ACT CGT CGA GTT GGT GAG JAF 402 * TTA ATG ATG ATG ATG ATG ATG GTA ACT GGA CTG CTG GGA TTT JAF 403 # this website GAG GAA TAA

TAA TTA ATA TTA TCA AGA AAA GAA A JAF 404 * TTA ATG ATG ATG ATG ATG ATG TTT GAT TAG TTT TTT GCT TA   #Underlined nucleotides indicate a manufacturer recommended addition to remove vector encoded N-terminal leader sequence for expression of the native protein.   *Underlined nucleotides indicate a manufacturer recommended addition to remove vector encoded C-terminal V5 epitope and add a polyhistidine tag for expression of the native protein. PI3K inhibitor plasmid construction Plasmids used in this study (Table 1) were constructed using the pBAD-TOPO® TA Expression Kit (Invitrogen, Carlsbad, CA) and initially cloned into One Shot® TOP10 E. coli. The E. coli CsrA complementation plasmid, pBADcsrAEC, was constructed by amplifying the endogenous E. coli csrA allele from MG1655 genomic DNA using primers JAF401 and JAF402. The resulting amplicon was then TA cloned into the pBAD-TOPO vector such that CsrA expression was inducible by arabinose and detectable for western blot analysis by the addition of a C-terminal hexahistidine selleck products tag. The C. jejuni complementation vector, pBADcsrACJ, was constructed by amplifying the C. jejuni csrA allele from 81–176 genomic DNA using primers JAF403 and JAF404

and cloning the resulting amplicon into pBAD-TOPO. Both complementation vectors and empty pBAD-TOPO plasmid were then transformed into the E. coli csrA mutant strain, TRMG1655, and recovered on LB agar containing ampicillin and kanamycin. In all phenotypic testing, we performed arabinose titration experiments (including samples without added arabinose)

to determine the dose-responsiveness of CsrA expression and complementation ability. Glycogen accumulation Glycogen accumulation was assessed using previously described methodologies [36]. Strains were grown at 37°C on Kornberg agar (1.10% K2HPO4, 0.85% KH2PO4, 0.6% yeast extract, 6-phosphogluconolactonase 1.5% agar) with or without 2% (v:v) glycerol or 2% (w/v) sodium pyruvate; either glycerol or pyruvate was used as a carbon source as opposed to glucose due to the inhibitory effect of glucose on the araBAD promoter [37]. Briefly, cultures were spotted on agar in the presence or absence of a carbon source and grown overnight at 37°C. Following incubation the cultures were stained by exposure to iodine vapor by inverting the plates over iodine crystals. Motility Motility was quantitated as previously described [38], inoculating semi-solid LB agar (0.35% agar) by stabbing with an inoculating needle dipped into overnight cultures and incubating for 14 hours at 30°C in a humidified incubator. After incubation, the diameter of the zone of motility was measured. Experiments were performed a minimum of three times with no fewer than three replicates per experiment.

Berthoux et al. [21] recently reported that Gd-IgA1 and IgA/IgG-IC may have a predictive value for outcome of renal death in IgAN. We examined these biomarkers from a perspective that is different from their study. The present study examined whether serum levels of these noninvasive biomarkers

can be a potential index for the disease activity of IgAN equivalent to urinalysis, in patients with complete or partial clinical remission after steroid pulse therapy in combination with tonsillectomy (TSP) whose clinical data and serum were selleck obtained 3–5 years after TSP. Materials and methods Patients and Androgen Receptor Antagonists treatment IgAN diagnosis requires renal biopsy with IgA as the dominant or co-dominant Igs in a typical mesangial distribution in the absence of clinical and laboratory evidence of systemic disease. We enrolled IgAN patients showing complete/partial clinical remission after TSP from 1999−2001 in Sendai Shakaihoken Hospital and who could be followed up and see more whose serum could be obtained serially for 3–5 years after TSP. Clinical remission was defined

as negative proteinuria and hematuria as assessed using a dipstick test and/or a urinary erythrocyte count of <5 cells per high-power field during 3 consecutive visits. We defined patients with complete remission as those who showed no further urinary abnormalities throughout the observation period after urinary abnormalities disappeared. Patients who exhibited a relapse of proteinuria and/or hematuria after remission were excluded from the complete remission group, but were included in a partial remission group. The steroid pulse therapy included 0.5 g methylprednisolone per day for 3

consecutive days, 3 times a week, for at least 1 week after tonsillectomy. Furthermore, 0.5 mg/body weight (kg) prednisolone was administrated once every 2 days for 6–12 months with a gradual tapering of the dose within 1 year [22]. Patients who had received a kidney transplant or who required dialysis were excluded from this study. This study was approved by the ethics committee of the Sendai Shakaihoken Hospital at Miyagi, Japan, and all patients provided written informed consent. Clinical, laboratory BCKDHA and pathological data We collected the baseline clinical data immediately before TSP, while qualitative hematuria and proteinuria data and serum were collected at a minimum of three time points, i.e., immediately before, 1 year after, and 3–5 years after TSP. Baseline clinical data (age, sex, duration from onset to tonsillectomy, systolic blood pressure, total protein, albumin, blood urea nitrogen, serum creatinine, creatine clearance rate [CCr], quantitative proteinuria, amount of proteinuria, and quantitative hematuria) and histological findings were collected from hospital medical records. CCr was calculated based on the mean 24-h urine collection and adjusted for body surface area.

Marco Camera is a specialist in Infectious Disease working at the IRCCS AOU San Martino-IST, Genoa Giovanni Orengo was medical director of San Martino-IST

Hospital until 2011 and then director of hospital hygiene to date. His main goal was to implement active microbiological surveillance systems and he’s director of the Committee for the fight against Nosocomial Infections. Claudio Viscoli is Full Professor of Infectious Diseases at the University of Genoa, Genoa, Italy. He is the head of the Infectious Diseases Unit, IRCCS AOU San Martino-IST, Genoa. He had BVD-523 published more than 100 international papers. Anna Marchese is Associate Professor 3-deazaneplanocin A price of Clinical Microbiology at the University of Genoa, Genoa, Italy. Her research fields include: epidemiology of mechanisms of antibiotic resistance, antimicrobial susceptibility testing, antimicrobial profile of

new drugs, bacterial genetics. She has published more than 80 international papers. Acknowledgements We would like to thank O. Varnier, Head of the Diagnostic Microbiology Unit. We gratefully acknowledge P. Gritti for her technical diagnostic assistance. References 1. Bonomo RA: New Delhi metallo-beta-lactamase and multidrug resistance: a global SOS? Clin Infect Dis 2011, 52:485–487.PubMedCrossRef 2. Nordmann P, Boulanger AE, Poirel L: NDM-4 metallo-β-lactamase with increased carbapenemase activity from Escherichia Bafilomycin A1 coli . Antimicrob Agents Chemother 2012, 56:2184–2186.PubMedCentralPubMedCrossRef 3. Dortet L, Poirel L, Anguel N, Nordmann P: New Dehli metallo- β-lactamase 4-producing Escherichia coli in Cameroon. Emerg Infect Dis 2012, 18:1540–1542.PubMedCentralPubMedCrossRef 4. D’Andrea MM, Venturelli C, Giani T, Arena F, Conte V, Bresciani P, Rumpianesi F, Pantosti A, Narni F, Rossolini GM: Persistent carriage and infection by multidrug-resistant Escherichia coli ST405 producing NDM-1 carbapenemase: report on the first italian cases. J Clin Microbiol 2011,49(Suppl 7):2755–2758.PubMedCentralPubMedCrossRef

5. Gaibani P, Ambretti S, Berlingeri A, Cordovana M, Farruggia P, Panico M, Landini MP, Sambri V: Outbreak of NDM-1-producing Enterobacteriaceae in northen Italy, July to August 2011. Euro Surveill 2011,16(Suppl Phosphoprotein phosphatase 47):20027.PubMed 6. The European Committee on Antimicrobial susceptibility testing: Breakpoint tables for interpretation of MIC’s and zone diameters. 2014.URL 7. Arakawa Y, Shibata N, Shibayama K, Kurokawa H, Yagi T, Fujiwara H, Goto M: Convenient test for screening metallo-β-lactamase-producing gram-negative bacteria by using thiol compounds. J Clin Microbiol 2000, 38:40–43.PubMedCentralPubMed 8. Yuan M, Aucken H, Hall LM, Pitt TL, Livermore DM: Epidemiological typing of Klebsiella with extended-spectrum β-lactamases from European intensive care units. J Antimicrob Chemother 1998, 41:527–539.PubMedCrossRef 9.

Our data found Nanog mRNA had the highest specificity

in lung cancer. We further confirmed the high diagnostic value of Nanog protein levels by IHC, Nanog was overexpressed in lung cancer tissues, but rarely expressed in non-malignant lung tissue. Taken together, these results demonstrate that Nanog mRNA is a potential diagnostic marker for lung cancer. Nanog is a transcription factor that plays an important role in maintaining self-renewal of embryonic stem cells. Current studies have reported that the expression of Nanog was higher in multiple cancerous tissues than in their normal counterparts, including breast cancer [20], gastric adenocarcinomas [21], colorectal cancer [22], gliomas [23] and ovarian serous cystadenocarcinomas [24]. In this study, we found the expression of Nanog Selleck PLX3397 mRNA in bronchoscopic biopsies of lung cancer patients was significantly higher compared to that in non-cancer patients. Although Nirasawa et al. [16] have also reported that the expression of Nanog mRNA was higher in surgically resected lung cancer tissues than in non-cancerous tissues, it is not known what cells express Nanog in non-cancerous lung

tissues. Using IHC, we found Nanog was only expressed in metaplastic P005091 squamous bronchial epithelium cells in 2 out of 50 non-malignant lung tissues, and was negative in normal airway epithelia. Therefore, Nanog may be a good diagnostic marker for lung cancer. In this study, our results showed that the mRNA levels of Bmi1, CD44 and CD133 were not

significantly different between lung cancer and non-malignant lung tissues. Further PI3K inhibitor analyzed by IHC, we observed that Bmi1, CD44 and CD133 were not only expressed in lung cancers, Bmi1 and CD44 were also abundantly expressed in lung interstitial cells, inflammatory cells and bronchial epithelium cells, and CD133 was diffusely expressed in some normal bronchial epithelium cells and bronchial smooth muscle cells, consistent L-NAME HCl with previous studies [11, 25, 26]. Hence, Bmi1, CD44 and CD133 are poor diagnostic markers for lung cancer. Likewise, although the expression levels of Sox2 and Msi2 mRNA in lung cancer tissues were significantly higher as compared with non-malignant tissues, we found more than 80% of bronchoscopic biopsy specimens of non-cancer patients were positive for Sox2 and Msi2 mRNA, and all non-malignant tissues were positive for Sox2 and Msi2 protein expression, consistent with previous findings [10, 27, 28]. Therefore, Sox2 and Msi2 have poor diagnostic specificity in lung cancer. It is still controversial whether lung cancer cells express OCT4.

[19] who reported that the antimicrobial agent produced by Pseudomonas species MCCB was stable after autoclaving at 121°C for 20 min even though there #AZD3965 purchase randurls[1|1|,|CHEM1|]# was a significant reduction in activity. Uzair et al. [20] also reported

the thermal stability of an antimicrobial agent produced by Pseudomonas aeruginosa at a temperature of 121°C for 20 minutes. However, Roitman et al. [21] showed that variations in the fermentation medium often results in changes in the composition of the antibiotics produced. The differences in the thermal stability of the antimicrobial agents produced in this study as compared to other studies may therefore be due to differences in some nutritional and or physical factors which led to the production of metabolites that are thermolabile at temperatures beyond 100°C. Our results also showed that nine days incubation period was optimum for maximum antibacterial activity by MAI2, an indication of maximum antibiotic production, after which there was no significant increase. Several other factors influence production of secondary metabolites by microorganisms, the most important one being the composition of the fermentation medium [22]. Sole et al. [23] noted that glucose can be used as a source for bacterial growth while repressing the production of secondary metabolites. The isolate (MAI2) utilised glycerol and starch best

for maximum production of the antimicrobial metabolites. Nitrogen is very vital in the synthesis of enzymes involved in primary and secondary metabolism Selleck BVD-523 [24]. Therefore depending on the biosynthetic pathways involved, nitrogen sources may affect antibiotic formation. Shapiro [25] noted that the type of nitrogen source (organic or inorganic) plays

a role in the synthesis of secondary metabolites. Phosphoprotein phosphatase Charyulu and Gnanamani [26] reported that Pseudomonas aeruginosa MTCC 5210 utilized organic nitrogen source for better yield of antimicrobial metabolites than the inorganic sources. These observations are consistent with the findings of this study as asparagine was better used for antibiotic production by MAI2 than the inorganic nitrogen sources (sodium and potassium nitrates and the ammonium salts) employed. Generally, the intracellular pH of most microorganisms is maintained near neutrality regardless of the pH in the outside medium [27]. However as the proton gradient across the cytoplasmic membrane increases, the cells commit more of their resources towards maintaining the desired intracellular pH [28], thus changes in external pH affect many cellular processes such as growth and the regulation of the biosynthesis of secondary metabolites [29]. The highest activity of the antimicrobial metabolite by the strain was at pH 7. This result agrees with a study carried out by Charyulu and Gnanamani [26] who reported maximum production of metabolite by Pseudomonas aeruginosa MTCC 5210 at pH 7.

Fold changes were calculated

for day 2 spherules vs mycelia and day 8 spherules vs mycelia. For each gene, the absolute peak log 2 fold change (FC) was identified across the three conditions and the raw expression values for the top 100 were log transformed and median-centered and included in the heatmap. Hierarchical clustering of genes and array samples based on their expression profiles is reflected in the dendrograms to the left and the top of the heatmap respectively and was performed selleck products by calculating distances using the Pearson correlation metric and then clustering distances using the average linkage method. The expression of genes marked with an asterisk (*) was confirmed by RT-qPCR. The scale is shown: red shading indicates greater expression blue shading represents lesser expression. Figure 3 Venn diagrams showing the number of genes that are differentially expressed in day 2 spherules and day 8 spherules compared to mycelia. The

number of up- or downregulated genes in shown. The procedures for determining up- or downregulation are in the methods section. There were a total of 2208 genes (22% of the genome) that were differentially expressed between spherules at one or both the time points we studied and mycelia. Figure  4 shows Venn diagrams depicting up- and downregulated genes in day 2 and day 8 spherules compared to mycelia. About a third of the differentially expressed

genes were up- or downregulated in both day 2 and day 8 spherules compared to mycelia. Florfenicol However, similar numbers of genes were exclusively upregulated in either selleck kinase inhibitor day 2 (N = 443) or day 8 (N = 319) spherules, or exclusively downregulated at either day 2 (N = 565) or day 8 (N = 233) spherules. The difference in gene expression between day 2 and day 8 spherules was apparent when we compared day 2 and 8 spherules directly to each other; 1,197 differentially expressed genes (12% of the total genome) were identified (Additional file 4: Table S2). Therefore, although gene expression by environmental form of the fungus and the parasitic form were quite distinct as might be expected, gene expression by young and mature spherules was also quite different from each other. Not only were there differences in which genes were expressed at each stage, but also the degree of modulation was large. For example, the maximum difference in expression of a gene (CIMG_10264) between day 2 spherules and mycelia was 48.6 fold and the median modulation between mycelia and day 2 spherules was 3.26. Figure 4 Confirmation of gene expression differences by RT-qPCR between day 2 spherules vs mycelia, day 8 spherules vs mycelia and day 8 vs day 2 spherules. The figure shows a comparison between the fold change for each gene for RT-qPCR data (grey bars) and microarray data (black bars) between the different conditions.

TCS and SI carried out the antigen identification by mass-spectrometry. CK and SK performed Compound C the deep sequencing analysis of the HCDR3. CSH and ARMB conceived the study, and participated in its design and coordination and helped to draft the manuscript. All authors read and approved the final manuscript.”
“Background Vibrio anguillarum, a highly motile

marine member of the γ-Proteobacteria, is one of the causative agents of vibriosis, a fatal hemorrhagic septicemic disease of both wild and cultured fish, crustaceans, and bivalves [1]. Fish infected with V. anguillarum display skin discoloration and erythema around the mouth, fins, and vent. Necrotic lesions are also observed in the abdominal muscle [2]. Mortality rates in infected fish populations range as high as 30-100% [1, 3]. Vibriosis has caused severe economic losses to aquaculture worldwide [1, 3] and affects many farm-raised fish including Pacific salmon, Atlantic salmon, sea bass, cod, and eel [3, 4]. V. anguillarum enters its fish host through the gastrointestinal tract (GI) and quickly colonizes this nutrient rich environment [2, 5]. Garcia et al. [6] have www.selleckchem.com/small-molecule-compound-libraries.html shown that V. anguillarum grows extremely well in salmon intestinal

mucus and that mucus-grown cells specifically express a number of different proteins, including several outer membrane proteins [6] and the extracellular metalloprotease EmpA [2, 5]. Several genes have been reported to be correlated with virulence by V. anguillarum, including the vah1 hemolysin cluster [7, 8], the rtx hemolysin cluster [9], the siderophore mediated iron transport system [10], the empA metalloprotease [2, 5], and the flaA gene [11]. Hemolytic activity of V. anguillarum has been considered

to be the virulence factor responsible for hemorrhagic septicemia during infection [10]. We have identified two hemolysin gene clusters in V. anguillarum that contribute to the virulence of this pathogen [8, 9]. One gene cluster, rtxACHBDE, encodes a MARTX toxin and its type I secretion system [9]. The second hemolysin gene cluster in V. anguillarum strain M93Sm contains the hemolysin gene Montelukast Sodium vah1 flanked by two putative lipase-related genes (llpA and llpB) immediately downstream and upstream by a divergently transcribed hemolysin-like gene (plp) that appears to function as a repressor of vah1-dependent hemolytic activity [8]. The plp-encoded protein has very high sequence similarity to phospholipases found in other pathogenic Vibrio species [8]. However, the enzymatic characteristics of Plp in V. anguillarum were not described. Generally, phospholipases are divided into several subgroups depending on their specificity for hydrolysis of ester bonds at different locations in the phospholipid molecule.

Exclusion criteria differed between FLSs; four excluded patients with pathological fractures and four with high energetic trauma (HET). Counselling of the fracture nurse was performed by the trauma surgeon in two FLSs, by an endocrinologist in three or by a rheumatologist or general internist in one FLS. Baseline characteristics (age, sex and CRFs) were screened during the visit at the FLSs by questionnaire before their visit

to the FLS in three centres and by personal contact with the nurse in two centres. In three centres, the patient filled in the questionnaire and discussed this at the outpatient clinic, in two centres all questions were asked by the nurse. CRFs were examined in all, but recording varied between FLSs. Whether patients had a history of fracture after the age of 50 years, GS-1101 order a family history of hip fracture or used glucocorticoids was recorded in >97% of

all patients. A history of vertebral fracture was asked for in all patients in four centres and in 65% of one centre. Low body weight was recorded as a CRF in >94% of patients in four centres and in 69% of patients in one centre. A fall during the past year was asked for in >99% of patients in three centres and in 44% in one centre. In one centre, the nurse inquired into previous falls in the preceding 6 months PAK5 (data not shown). RXDX-101 clinical trial DXA examinations were performed in 83 up to >99% of patients. Criteria for laboratory examinations differed between FLSs: in all patients (n = 1), only in men (n = 1), in men younger than

65 years (n = 2), in patients with a T-score <−2.0 (n = 1), and in women depending on age and T-score (n = 2) (Table 1). The acute circumstances of trauma were specified in all FLS, but extensively in four (Table 2). Table 2 Prevalence of CRFs, falls and circumstances of trauma in all patient cohorts and according to the different FLSs   1 2 3 4 5 All RRa P valueb Age (SD) 67.5 (10.7) 69.0 (10.5) 65.6 (9.3) 65.4 (9.2) 67.0 (10.2) 66.7 (10.0)   <0.001 Sex (%)               <0.001  • Women 74.2 88.2 70.0 79.9 77.0 76.7      • Men 25.8 11.8 30.0 20.1 23.0 23.3     Fracture location (%)               <0.001  • Major 18.1 15.3 13.4 14.6 14.8 15.5      • Minor 70.3 78.5 66.3 65.5 75.9 70.1      • Hip 5.5 5.3 7.6 7.3 1.0 5.7      • Fingers/Toes 6.1 0.9 12.6 12.6 8.4 8.7      • Hip 5.5 5.3 7.6 7.3 1.0 5.7      • Humerus 13.7 12.3 9.9 11.0 14.3 12.2      • Distal radius/ulna 25.8 22.4 26.8 26.9 27.2 26.1      • Tibia/fibula 12.7 12.8 13.3 12.7 12.8 12.9      • Other 42.3 47.1 42.4 42.1 44.7 43.2     BMD (%)               <0.001  • Normal BMD 23.7 5.0 26.6 15.5 30.3 21.2      • Osteopenia 44.7 54.3 46.2 45.5 47.5 46.6      • Osteoporosis 31.6 40.7 27.2 39.0 22.2 32.

The genes espA espB and espD are found within the LEE4 operon of EPEC [13, 14]. Evidence suggests that zinc dependent down regulation of LEE4 involves the global regulator protein Ler, encoded within the LEE1 operon. Zinc also reduces expression of LEE1, and thus Ler [11].

In our current study we sought to understand the underlying mechanism of how zinc reduces the expression of LEE genes of EPEC. We found no evidence to suggest that zinc directly acts on the regulatory protein Ler. Rather, we present evidence that zinc causes EPEC envelope stress, leading to a σ E-dependent stress response characterized by increased expression of rpoE. Treating EPEC with ammonium metavanadate (NH4VO3) – a known chemical inducer of the σ E-dependent response

– caused a reduction in type III-dependent secretion Protein Tyrosine Kinase inhibitor similar to that observed in the presence of zinc. This is a first account of a specific mechanism on how zinc supplements reduce the duration and severity of disease caused by EPEC and related diarrhoeal pathogens. Results Millimolar concentrations of zinc are required to inhibit Ler binding Previous studies indicated that exogenous zinc diminished EPEC pathogenesis, in part, by inhibiting expression of virulence genes. Specifically, expression of genes of the LEE, encoding components of the type III secretion system, were reduced in the presence of 0.1 to 0.5 mM zinc acetate [11, 15]. Data suggested that, for the LEE4 operon, encoding espA, zinc-dependent

down-regulation OICR-9429 required the global regulator Ler [14], which controls expression of the LEE4 operon. Thus we initially posited that upon zinc stress cytoplasmic concentrations of this metal ion prevented Ler binding to LEE4 regulatory DNA. To test this hypothesis, we performed electrophoretic mobility shift assays (EMSA) using purified components (Figure 1). One hundred nanograms of LEE4 regulatory DNA was incubated with 500 nM Ler protein with increasing amounts of zinc acetate. In the absence of added zinc, the Ler/DNA complex migrated poorly into the polyacrylamide gel compared to the DNA fragment alone, consistent with previously published data [16, 17]. Concentrations of added zinc acetate up to 100 μM showed no buy Atezolizumab effect on the ability of Ler protein to bind and shift the LEE4 regulatory DNA (Figure 1). At 1000 μM, or 1 mM, zinc acetate we observed reduction in the ability of Ler to bind LEE4 DNA by 80%. Thus in vitro, millimolar concentrations of zinc were necessary to disrupt Ler binding to regulatory DNA sequences. Figure 1 Sub-millimolar zinc does not interfere with Ler binding to the  LEE4  operon in vitro. Ler binding to a fragment containing the LEE4 promoter (bases -468 to +460 relative to the transcription start point) was assessed by EMSA in the presence of varied zinc acetate concentrations.

The interview is followed by an Epilogue that describes previously undisclosed details surrounding a manuscript Benson completed just before leaving Berkeley for Penn State. The video and the transcript have been posted on You Tube (http://​youtu.​be/​GfQQJ2vR_​xE). BEGINNING OF

VIDEO Buchanan: I’m at the Scripps Institution of Oceanography in La Jolla, with Andrew Benson, where he is an emeritus professor of biology. We are in an office Dr. Benson has occupied since he arrived at Scripps in 1962. In today’s interview, Andy, I would like to discuss your career, focusing on research that led to the discovery of the Calvin–Benson cycle in photosynthesis, a pathway essential to the growth of all plants. This work was done in collaboration with the late Melvin Calvin in the Chemistry Department at Berkeley.

Andy, for today’s purposes, we will start early in your life with your arrival as a freshman at Berkeley. Andy, you RGFP966 cost arrived in Berkeley in 1935 as a young chemistry major. Why did chemistry interest you?   Benson: Because in high school I had an excellent—a very interesting chemistry teacher. He had been on the football team of Stanford University. And he was a big guy. And everyone was afraid of him. (laughs). But he had—did some tricks that really fooled everybody.   Student days see more Buchanan: So that was one of the attractions. Well, after you arrived in Berkeley, your father took you to meet Wendell Latimer, a well-known chemist who was chairman of the Chemistry Department. What were your first impressions of the campus after you arrived as a youth, fresh from central California?   Benson: Well, it was full of people (laughs) and they all knew where they were going.   Buchanan: (laughs)

  Benson: And I was only going to hopefully find the Chemistry Department.   Buchanan: Well, after completing your Bachelor’s degree, you continued as a chemistry graduate student at Cal Tech, where you worked with Carl Niemann, one of the nation’s most distinguished chemists. What was Professor Niemann’s specialty?   Benson: He was a specialist in carbohydrate chemistry, anything involving sugar molecules and plastics and everything. He—his lectures, for over three years, were brilliant. And he was a well known—chairman of the chemistry—chemists of the National Academy of Sciences.   As a young Ph.D. in Berkeley Buchanan: This training provided excellent preparation for the research you were to carry out following your return to Berkeley as a young Ph.D. in 1942. At that time, there was great activity in chemistry at Berkeley. What was the Chemistry Department like in 1942?   Benson: I was in charge of several sections of the teaching groups in chemistry.   Buchanan: So this was your role as a faculty member.   Benson: Yeah. And the students in those two groups that I managed were absolutely at the top of the students, as far as their test scores went.