CSHL press; 2000:1.32–1.37. 24. Pidiyar VJ, Jangid K, DZNeP in vitro Patole MS, Shouche YS: Studies on cultured and uncultured microbiota of wild Culex quinquefasciatus mosquito midgut based on 16s ribosomal RNA gene analysis. AmJTrop Med Hyg 2004, 70:597–603. 25. Miller JM, Rhoden D: Preliminary Evaluation of Biolog, a Carbon Source Utilization Method for Bacterial Identification. click here Journal Of Clinical Microbiology 1991,29(6):1143–1147.PubMed 26. Murray AE, Hollibaugh JT, Orrego C: Phylogenetic comparisons of bacterioplankton from two California estuaries compared by denaturing gradient gel electrophoresis of 16S rDNA fragments. Appl

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JC, Jones AJ, Weightman AJ: New Screening software shows that most recent large 16S rRNA gene clone libraries contain chimeras. Appl Environ Microbiol 2006,72(9):5734–5741.PubMedCrossRef 30. Schloss PD, Handelsman J: Introducing DOTUR, a computer program for defining operational taxonomic units and estimating species richness. selleck chemical Appl Environ Microbiol 2005,71(3):1501–6.PubMedCrossRef 31. Tamura K, Dudley J, Nei M, Kumar S: MEGA4: Molecular Evolutionary Genetics Analysis (MEGA) software version 4.0. Mol Biol Evol 2007,24(8):1596–1599.PubMedCrossRef 32. Saitou N, Nei M: The neighbor-joining method: A new method for reconstructing phylogenetic trees. Mol Biol Evol 1987, 4:406–425.PubMed 33. Kimura M: A Simple Method for Estimating the Evolutionary Rate of Base Substitutions

Through Comparative Studies of Nucleotide Sequences. J Mol Evol 1980, 16:111–120.PubMedCrossRef 34. Aziz RK, Bartels D, Best AA, DeJongh M, Disz T, et al.: The RAST Server: rapid annotations using subsystems mafosfamide technology. BMC Genomics 2008, 9:75.PubMedCrossRef 35. Arumugam M, Raes J, Pelletier E, Le Paslier D, Yamada T, et al.: Enterotypes of the human gut microbiome. Nature 2011,473(7346):174–80.PubMedCrossRef 36. Pandey PK, Siddharth J, Verma P, Bavdekar A, Patole MS, Shouche YS: Molecular typing of fecal eukaryotic microbiota of human infants and their respective mothers. J Biosci 2012, 37:221–226.PubMedCrossRef 37. Balamurugan R, Janardhan HP, George S, Raghava VM, Muliyil J, Ramakrishna BS: Molecular Studies of Fecal Anaerobic Commensal Bacteria in Acute Diarrhea in Children. J Pediatr Gastroenterol Nutr 2008, 46:514–519.PubMedCrossRef 38.

Considering the excellent selectivity

and the chemical stability of the supports bearing cationic lipid membranes of N-octadecylchitosan, their practical use as separation media in pharmaceutical manufacturing can be expected. Acknowledgements The author thanks Mr. Tsuneyasu Adachi and Mr. Jun-ichi Ida (Kurita Water Industries) for the valuable technical assistance. References 1. Kim Y-R, Jung S, Ryu H, Yoo Y-E, Kim SM, Jeon T-J: Synthetic Thiazovivin biomimetic membranes and their sensor applications. Sensors 2012, 12:9530–9550.ARRY-438162 research buy CrossRef 2. Stibius K, Bäckström S, Hélix-Nielsen C: Passive transport across biomimetic membranes. In Biomimetic Membranes for Sensor and Separation Applications. Edited by: Hélix-Nielsen C. New York: Springer; 2012:137–155. 3. Westphal O, Lüderitz O: Chemical research on lipopolysaccharides of Gram-negative bacteria. Angew Chem 1954, 66:407–417.CrossRef 4. Westphal O, Lüderitz O, Galanos C, Mayer H, Riestschel ET: The story of bacterial endotoxin. In Advances in Immunopharmacology 3. Edited by: Chedid L, 4EGI-1 mouse Hadden JW, Speafiro F. New York: Pergamon; 1986:13–34.CrossRef 5. Magalhäst PO, Lopes AM, Mazzola PG, Rangel-Yagui C, Penna TCV, Pesspa A Jr: Methods of endotoxin removal from biological preparations: a review. J Pharm Pharmaceut Sci 2007, 10:338–404. 6. Shibatani T, Kakimoto T, Chibata I: Purification of high molecular weight urokinase from human urine and comparative study of two active

forms of urokinase. Thromb Haemostasis 1983, 49:91–95. 7. Matsumae H, Minobe S,

Kindan K, Watanabe T, Sato T, Tosa T: Specific removal of endotoxin from protein solutions by immobilized histidine. Biotechnol Appl Biochem 1990, 12:129–140. 8. Issekutz AC: Removal of Gram-negative endotoxin from solutions by affinity chromatography. J Immunol Methods 1983, 61:275–281.CrossRef 9. Sakata M, Inoue T, Todokoro M, Kunitake M: Limulus amebocyte lysate assay for endotoxins by an adsorption method with polycation-immobilized cellulose beads. Anal Sci 2010, 26:291–296.CrossRef 10. Wakita M, Hashimoto M: Covalent immobilization of polymeric bilayer membranes to porous supports. Langmuir 1995, 11:4013–4018.CrossRef 11. Wakita M, Adachi T, Ida J, Hashimoto M: Selective adsorption of lipopolysaccharide from protein solutions by porous supports bearing cationic lipid membranes. Bull Chem Soc Jpn 1996, 69:1017–1021.CrossRef 12. Wakita M, Hashimoto Celecoxib M: Bilayer vesicle formation of N -octadecylchitosan. Jpn J Polymer Sci Technol 1995, 52:589–593. 13. Shands JW Jr, Graham JA, Nath K: The morphologic structure of isolated bacterial lipopolysaccharide. J Mol Biol 1967, 25:15–21.CrossRef 14. Aida Y, Pabst M: Removal of endotoxin from protein solutions by phase separation using triton X-114. J Immunol Methods 1990, 132:191–195.CrossRef 15. Wakita M, Hashimoto M: Selective adsorption of lipopolysaccharide in protein solution by polyion-complexed lipid membrane. Influence of the membrane rigidity on the adsorption selectivity. Langmuir 1995, 11:607–611.

Biochim Biophys

Acta 1983, 737:51–115.PubMed 61. Radolf JD, Bourell KW, Akins DR, Brusca JS, Norgard MV: Analysis of Borrelia burgdorferi membrane architecture by freeze-fracture electron microscopy. J Bacteriol 1994, 176:21–31.PubMed Authors’ contributions TL carried out the experiments for Figures 2, 3, 4, 5 and 6A-C and drafted the initial manuscript. MK participated in the design of the studies and performed experiments for 6D and provided intellectual input and editing assistance for the manuscript. XY and UP provided the data for Figure 1. DA conceived of EGFR inhibitor the study, participated in its design and coordination, and helped to draft and edit the manuscript. All authors read and approved the final manuscript.”
“Correction learn more After publication of this work [1], it came to our attention that the grant numbers in the Acknowledgements section were incorrect. This work was supported by two grants from Polish Ministry of Science and Higher Education

(No. N303 341835 and N401 183 31/3968) and by intramural grant of University of Warsaw (BW 19126). References 1. Grabowska AD, Wandel M, Lasica AM, Nesteruk M, Roszczenko P, Wyszynska A, Godlewska R, Jagusztyn-Krynicka EK: Campylobacter jejuni dsb gene expression is regulated by iron in a Fur-dependent manner and by a translational coupling mechanism. BMC Microbiol 2011, 11:166.PubMedCrossRef”
“Background Listeria monocytogenes is a ubiquitous gram-positive opportunistic pathogen that can cause very serious food-borne infections in humans, with symptoms including meningitis, frequently accompanied by septicemia and meningoencephalitis, which are particularly severe for newborns and immunocompromised individuals [1]. The antibiotics of choice in the treatment of listeriosis are the β-lactams penicillin G or ampicillin, alone or in combination with an aminoglycoside [2]. Olopatadine The classical target enzymes for β-lactam antibiotics are the penicillin binding proteins (PBPs). In L. monocytogenes, five PBPs were initially identified using radiolabeled β-lactams [3], and among

these, PBP3 was thought to be the primary lethal target due to the observed low affinity of β-lactams for this protein and excellent correlation between the MICs of different β-lactams and their affinity for this protein [4–6]. Further evidence that PBP3 is the primary target for active β-lactams is that only this PBP appears to be identical in all Listeria spp., and blockage of this protein has lethal consequences for the bacterial cell [7]. Recent in silico analysis of the L. monocytogenes EGD genome revealed the presence of 10 genes encoding putative penicillin binding proteins and find more subsequently nine of these were positively verified as PBPs by the binding of a fluorescent β-lactam derivative [8, 9].

The excitation spectrum of fluorescence in PSII is primarily dependent on the photosynthetic pigment composition, which distinguishes the major phytoplankton groups and, with exceptions, clearly separates cyanobacteria from algae (Fig. 2). Blue-green illumination (<550 nm) excites stronger fluorescence in algal cultures than

in cyanobacteria (Yentsch and Yentsch 1979; Vincent 1983; Schubert et al. 1989). Longer wavelength illumination favours cyanobacterial fluorescence but algal fluorescence remains significant. If the emission band is located at its optimum AZD5153 cost of 680–690 nm, as we recommend, the maximum excitation wavelength is practically limited to approximately 650 nm to prevent stray light from the excitation source reaching the detector. There is thus a relatively large section of the photosynthetically active spectrum where algal fluorescence dominates. A ‘white’ illumination source (Fig. 12a), for example, leads to a bias against cyanobacterial representation

https://www.selleckchem.com/products/LY2603618-IC-83.html in community fluorescence. In contrast, a ‘broad-green’ light source (Fig. 12b) that excites predominantly accessory photosynthetic pigments yields near-equal representation of algal and cyanobacterial F v/F m. Our results show a relatively low correlation coefficient (R 2 = 0.33) of the community F v/F m with either group in the community, when we simulate the broad-green light source. Of course, many of the randomly mixed communities combine cultures exposed to widely different growth conditions and with very different F v/F m at a specific excitation-waveband pair, so that the community signal could never represent both subcommunities equally in these cases. The approach of simulating community fluorescence is, therefore, not to be used to selleck chemicals interpret fluorometer performance beyond describing how well each group is represented in the community signal. In theory, the broad-green illumination band should predominantly excite accessory photosynthetic pigments, so that those phytoplankton groups that respond positively to the environmental conditions by producing accessory pigments, will dominate the result. This

idea warrants further study, particularly in natural environments where such Adenosine triphosphate information may be desirable. For multi-channel configurations, two narrow excitation bands located in the blue and orange-to-red constitute the minimum required combination to resolve some degree of subcommunity variable fluorescence information. Algal variable fluorescence is obtained with high accuracy from the blue channel. The extent to which orange excitation subsequently yields a different F v/F m will give some indication of the variable fluorescence of cyanobacteria in the community. This result is not unambiguous, because equal F v/F m from both blue and orange-excited fluorescence can be interpreted as equal F v/F m in algae and cyanobacteria but also as the absence of fluorescence from cyanobacteria.

There was sufficient DNA from twenty-one vaginal swabs to pursue the www.selleckchem.com/products/blasticidin-s-hcl.html molecular probe method as assayed on Tag4 arrays. Of these, there were fourteen DNAs sufficient to additionally pursue the molecular probe method as assayed by SOLiD sequencing. The complete results for all swabs are given in Table S2 (Additional

selleck screening library file 1). We present three examples here (Table 2). For clinical sample A08-2, BigDye-terminator sequencing of the 16S ribosomal RNA gene (rDNA) identified two bacteria for which there were molecular probes: L. crispatus and L. jensenii, in substantially different amounts (Table 2). The same two bacteria were also identified by molecular probe technology as assayed on both Tag4 arrays and by SOLiD sequencing. Based upon the BigDye-terminator data, neither assay produced false

negatives or false positives with this clinical sample. (We cannot distinguish the L. jensenii probes hybridizing with L. jensenii DNA, cross-hybridizing with L. crispatus DNA, or this website both.) Thirty-seven and thirty-eight bacteria were correctly negative with the Tag4 and SOLiD assays, respectively. Table 2 Clinical samples: comparison of BigDye-terminator reads, Tag4 fluorescent signals, and SOLiD reads. A08-2       Bacterium BigDye-terminator reads (%) Probes/Tag4 Probes/SOLiD L. crispatus 95% 1 1 L. jensenii < 1% 1 1 A10-4 Bacterium BigDye-terminator reads (%) Probes/Tag4 Probes/SOLiD L. crispatus 89% 1 1 L. gasseri < 1% 0 0 A22-3 Bacterium BigDye-terminator reads (%) Probe/Tag4 Probe/SOLiD E. faecalis   1 0 L. crispatus

86% 1 1 L. jensenii 13% 1 1 T. pallidum   0 1 The BigDye-terminator data are from [5]. For the purposes of this table, those bacteria whose presence was supported by less than ten BigDye-terminator reads have been ignored. Novel bacteria and bacteria without a public genome sequence have also been ignored because they cannot be detected by the molecular Carnitine dehydrogenase probes. “”1″”, a majority of molecular probes for this genome was positive. “”0″”, a majority of molecular probes for this genome was not positive For clinical sample A10-4 (Table 2), BigDye-terminator sequencing of rDNA identified two bacteria for which there were molecular probes: L. crispatus and L. gasseri, in substantially different amounts. Both assays detected L. crispatus, but neither assay detected L. gasseri. Clearly, the L. gasseri molecular probes had not cross-reacted with L. crispatus DNA. We assume that the amount of L. gasseri DNA in clinical sample A10-4 was below the minimum detection limit of the molecular probes, although the minimum detection limit of the molecular probes in clinical samples has not been determined and was probably different for each probe [2]. (The same assumption has been made in an additional six cases: four with the Tag4 assay and two with the SOLiD assay.) Thirty-seven and thirty-eight bacteria were correctly negative with the Tag4 and SOLiD assays, respectively.

Figure 1 Timeline of experimental procedures. Each participant participated in two experimental trials, one for each treatment, separated SN-38 chemical structure by at least one week for supplement wash out and recovery. During each trial participants were assigned to either: (a) 15 days oral ingestion of placebo; or (b) 15 days oral ingestion of 400 mg ATP/d with the Lazertinib dosage divided into two equal dosages, one in the morning and the other in the evening. All of the participants were classified as healthy and were not currently taking

prescription medications or other dietary supplements. Multi-vitamins not exceeding the RDA were allowed. None of the participants were classified as competitive athletes or currently participated in daily heavy physical work or weight training. Participants had to be able to perform the fatigue testing and also were required to commit to maintaining their current activity levels throughout the study. Participants also had to agree to repeat a consistent dietary intake for the 24-hour period before each of the testing protocols. Participants

not able to meet the inclusion criteria were excluded from the study. All procedures involving human participants were approved by the Iowa State University Institutional Review Board, and written informed consent was obtained from all participants prior to participation. For each of the trials, participants refrained from vigorous exercise for three days before selleck screening library reporting to the laboratory in the morning after an overnight fast (Figure 1). Exercise consisting of light stretching and/or mild aerobic exercise lasting less than 45 minutes was allowed during this pre-study period. At this time, a blood sample was obtained. Weight and height were measured and BMI was calculated. Additionally, for characteristic purposes only, body composition was measured using air displacement plethysmography

however (BodPod®, Life Measurements, Concord, CA). The participants were then given their first week supply of blinded capsules with instructions on proper dose scheduling and completion of a dose-log. Participants returned to the laboratory after the first week to receive their second week of capsules and to confirm their compliance with the dosing schedule; there were no training or nutrition journals recorded. At the end of the 15 days of dosing, the participants returned to the laboratory for post-supplementation testing. Another blood sample was taken and the participant’s body weight was again measured and BMI calculated. The participants were allowed to recover from the blood sampling for at least 30 min and then the strength/fatigue testing measurements were taken. No supplement was given before testing and all testing was conducted after an overnight fast and after three days of exercise restriction as in the preliminary testing.

The control animals were instilled with 50 μL of sterile pyrogen-free water. Correct insertion of the tube into the trachea was assured by using a modified pneumotachometer (National Research Centre for the Working Environment, Copenhagen, Denmark)

[12]. To establish a time-response relationship (experiment 4), 10 mice per dose were exposed Selleckchem eFT508 by i.t instillations to either 3.4 × 106 CFU Vectobac® or 3.5 × 105 CFU Dipel®. BAL fluids were collected 4 hours, 24 hours or 4 days post GS1101 exposure and cells were counted and differentiated as described below. Subsequently, in order to establish a dose-response relationship (experiment 3), 10 mice per dose was exposed by i.t instillations to a Vectobac® dose of 1.25 × 104, 2 × 105, 4.2 × 105 or 1.2 × 106 CFU, respectively. BAL fluids were collected 24 hours post exposure and cells were counted and differentiated as described below. For the sub-chronic study (experiment 5) the instilled doses were 3.4 × 106 CFU for Vectobac® and 3.5 × 105 for Dipel®. Repeated aerosol inhalations (experiment 6) Mice (n = 9 per group) were inserted into body plethysmographs that were connected to the exposure chamber. The respiratory parameters were obtained

for each mouse from a Fleisch pneumotachograph connected to each plethysmograph that allows continuously monitoring of the parameters [13, 14]. The exposures were preceded by a period that allowed the mice to adapt to the plethysmographs. Then, a 15 min. period was used to establish baseline (control) values of the respiratory parameters. LY333531 datasheet This period was followed by a 60 min. exposure period and a 15 min recovery period. Mice were exposed 60 min/day for 5 days per week for two weeks with a two-day break in-between. The dose of 5 × 104 CFU per mouse per exposure was chosen to mimic occupational exposure [15]. Suspensions of bacteria were delivered from a glass syringe, administered by an infusion pump (New England

Medical Instruments Inc., Medway, MA, USA) and via a polyethylene tube connected to a Pitt. No. 1 aerosol generator [16]. The aerosol was mixed through a Vigreaux-column and led to a glass/stainless steel exposure chamber as described Sodium butyrate [17]. Total flow rate through the chamber was 20 L/min and the air input through the aerosol generator was 14 L/min. The aerosol generator and all related equipments were thoroughly cleaned between exposure sessions. During the aerosol exposures, air samples were collected from the breathing zone of the mice for determination of particle size distribution, real-time particle counts and aerosol CFU concentration. This was done by APS at a flow of 5 L/min, LHPC at 2 L/min and by a filter method GSP at 3.5 L/min. The APS monitored the size distribution of particles in the range from 0.542 to 19.81 μm (aerodynamic diameter) in the exposure chamber. Real time particle counts in the exposure chamber was counted by LHPC in the ranges 0.7-2.

B. pseudomallei isolates are genetically quite diverse [4, 5], and this heterogeneity may be due at least in part to the highly variable distribution of bacteriophages among strains [6]. Such differences may provide certain strains

survival advantages in the environment and the host, as well as explain the variable clinical presentation of melioidosis. Also raising concern as a Torin 1 ic50 potential biological weapon is the very closely related B. mallei, causal agent of the primarily equine disease known as glanders [7]. In contrast to B. pseudomallei, B. mallei is a highly specialized pathogen, not found outside of a mammalian host in nature. B. mallei is a host-adapted clone of B. pseudomallei, and all of the selleck inhibitor B. mallei genome is nearly identical VS-4718 molecular weight to a set of genes within B. pseudomallei core genome. However, in addition to its core genome B. pseudomallei contains numerous contiguous gene clusters that were deleted from B. mallei during its evolution [8, 9]. B. thailandensis is another closely related organism often found in the same environmental samples (soil and water

of endemic melioidosis regions) as B. pseudomallei [10]. Unlike B. pseudomallei and B. mallei, B. thailandensis has very low virulence in most animal hosts, including humans. The ability to metabolize arabinose, and the corresponding loss of the arabinose assimilation operon from B. pseudomallei, phenotypically distinguishes B. thailandensis from B. pseudomallei [11]. The genes encoding arabinose assimilation may be considered as antivirulent, and their absence from B. pseudomallei (and B. mallei) may have allowed the development of the latter as pathogens [12]. Burkholderia

multivorans, a member of the Burkholderia cepacia complex, is an opportunistic pathogen associated with infection in cystic fibrosis patients that is also found in soil environments ID-8 [13]. The presence of prophages among bacterial isolates and their possible contribution to bacterial diversity is widespread. By carrying various elements contributing to virulence, prophages can contribute to the genetic individuality of a bacterial strain. This phenomenon has been reported in Salmonella spp [14] and Lactobacillus spp [15, 16], among others. Prophage-associated chromosomal rearrangements and deletions have been found to be largely responsible for strain-specific differences in Streptococcus pyogenes [17] and Xylella fastidiosa [18]. Thus, temperate phages carrying foreign DNA can play a role in the emergence of pathogenic variants. Lateral gene transfer between phage and host genomes, and phage lysogenic conversion genes, can alter host phenotype through production of phage-encoded toxins and disease-modifying factors that affect virulence of the bacterial strain.

2001; Alia et al. 2001, 2004; van Gammeren et al. 2004, 2005a, b; Ganapathy et al. 2007) and reaction center complexes (Prakash et al. 2005; Diller et al. 2007; Daviso et al. 2008; Alia et al. 2009) have been GSK2399872A solubility dmso resolved with atomic resolution using MAS NMR in conjunction with stable-isotope labeling. Very recently, the structure of a member of the chlorosome class of Pexidartinib mouse light-harvesting antennae was determined and compared with the wild type (WT) to resolve how the biological light-harvesting function of the chlorosome is established, an important step on the way to artificial photosynthesis

(Ganapathy et al. 2009). This article is devoted to summarize the research into the direction of comprehensive protein assessment using the LH2 antenna system as a model protein using MAS NMR. First, a brief theoretical background of the MAS NMR technique is presented. Subsequently, a variety of model experiments performed

by MAS NMR for LH2 complex will be discussed to illustrate the versatility of MAS NMR as a biophysical technique in photosynthesis. Theoretical background MAS NMR is a technique for obtaining high resolution NMR data from solids. For an extensive introduction to the technique, the reader is referred to the existing literature (Duer 2004). This section serves to guide the interested student to this background literature. Contrary to solution NMR, where anisotropic interactions are averaged by the rapid tumbling of molecules, in solid-state NMR, interactions such as

the FK228 chemical shift and dipolar coupling dominate. As a consequence, the spectral line width of nuclei in solids is Idoxuridine rather broad. In order to overcome this problem in the solid state, MAS NMR is applied. In MAS NMR, a sample is rotated rapidly around an axis at the magic angle θ m = 54.74° with the static field (Andrew et al. 1958; Lowe 1959) to effectively suppress chemical shift broadening. In order to describe the MAS NMR experiment, the Hamiltonian $$ H = H_\textCS + H_\textD^IS + H_\textD^II $$ (1)is used. \( H_\textCS \) is the chemical shielding term, \( H_\textD^IS \) represents the heteronuclear dipolar couplings, and \( H_\textD^II \) describes the homonuclear dipolar couplings. The chemical shielding affects the NMR frequency, which is determined by the Zeeman interaction $$ H_ 0 = – \mu \cdot \mathbfB_ 0 , $$ (2)between a nuclear magnetic moment μ and the external static magnetic field \( \mathbf\bf B_ 0 \). The μ can be expressed in terms of the nuclear spin operator I as \( \mu = \gamma \hbar \mathbfI_{{}} \), and Eq. 2 can be rewritten as $$ H_ 0 = – \gamma \hbar I_z B_ 0 .

CT scan findings of gut malrotation and small bowel obstruction without volvulus, may show internal herniation secondary to Ladd’s bands. Mesenteric angiography was previously used but is now

rarely indicated in the evaluation of malrotation. It has the capacity to demonstrate the abnormal relationship between, and detect the patency of, the mesenteric vasculature. Angiography was used to demonstrate the characteristic corkscrew appearance of a whirling SMA and its branches; the ‘barber pole sign’ as well as extensive collaterals caused by proximal SMA occlusion [16]. However, its role has been superseded by the CT scan which has the overall advantage of not only detecting the abnormal location of the midgut but also the reversed mesenteric anatomical relationship as well as any other intra-abdominal anomalies associated with malrotation. PF-573228 nmr Symptomatic MK-0457 midgut malrotation undoubtedly requires surgical intervention although the management of asymptomatic patients is more controversial. Choi et al [17] reviewed 177 patients over a 35-year period. They found that asymptomatic patients had a low risk of intestinal volvulus and therefore advised that routine ABT-263 in vitro investigations, screening and elective surgery were not necessary with close follow-up. However, it is

increasingly argued that all suitable patients with intestinal malrotation should undergo surgical correction regardless of age as it is impossible to predict which patients will develop catastrophic complications [8]. Several small case series have recommended that elective Ladd’s procedure should be performed

in all patients with intestinal malrotation. The authors of the studies that include cases of life threatening small bowel ischaemia argue this point particularly strongly [3, 5, 7, 9]. Of course, the operative policy should be based on the presentation and suspected diagnosis; the potential risks of the procedure need to be weighed against the benefits. The surgical management of intestinal malrotation was first described by William Ladd in 1936 [6] and this remains the mainstay of treatment. The classical Ladd’s Procedure consists of 4 parts: division of Ladd’s bands overlying the duodenum; widening of the narrowed root of the small bowel mesentery by mobilising the duodenum and Quisqualic acid division of the adhesions around the SMA to prevent further volvulus; counterclockwise detorsioning of the midgut volvulus if present and appendicectomy to prevent future diagnostic dilemma of an abnormally located appendix [6]. The original Ladd’s procedure was described for the paediatric population group and the full components of this procedure may not be offered in the adult group [4–6, 9]. Most authors are of the opinion that Ladd’s procedure is an adequate treatment for intestinal malrotation. Fu et al [7] reported a complete resolution of symptoms in 9 and near complete resolution in 2 of 11 patients.