Chemicals Inc Research Articles

Single name unites Air Products’ membrane business units

US-based Air Products and Chemicals Inc, which sells gases and chemicals for industrial uses, recently announced a new brand identity for its membrane business units, which now all operate worldwide as Air Products Membrane Solutions.

Air Products and Chemicals Inc.

Air Products and Chemicals Inc.

Energy efficiency enhancement of mixed refrigerant process in LNG plant

The liquefaction natural gas (LNG) process is one of the most important thermodynamic processes in the cryogenic gas industry. The operating conditions change during the compression process, throttling and heat transfer, changing the thermodynamic properties of the natural gas (NG) and refrigerants in the major equipments, including cryogenic compressors, expanders, coolers and heat exchangers. To improve the energetic efficiency of LNG plant, a thermodynamic analysis by the exergetic method was used. Energy equilibrium equations and exergy equilibrium equations of each equipment in the Air Products and Chemicals Inc (APCI) process were established. This paper is limited to the exergy analysis of the mixed refrigerant (MR) components: the axial and centrifugal compressors and the main cryogenic heat exchanger. The results show that the inlet temperature and inlet pressure of MR compressors has an impact on the evolution of the exergy efficiency. For a process MR, axial compressor is the main equipment contributing to total exergy losses.

Corporate Profiles

Corporate Philanthropy ReportVolume 33, Issue 9 p. 4-11 Corporate Profiles Corporate Profiles First published: 16 August 2018 https://doi.org/10.1002/cprt.30224Read the full textAboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onFacebookTwitterLinkedInRedditWechat Abstract Air Products and Chemicals Inc. SpartanNash Co. Andeavor SUPERVALU Inc. Edison International Stryker Corp. The Estée Lauder Companies Inc. Waste Management Inc. BorgWarner Inc. Volume33, Issue9September 2018Pages 4-11 RelatedInformation

Harcros Chemicals Inc announces SaferChoice approval of H-Quest and T-Det products for CleanGredients listing

Harcros Chemicals Inc announces SaferChoice approval of H-Quest and T-Det products for CleanGredients listing

Corporate Profiles

The Boeing Co. The Home Depot Inc. Macy's Inc. Las Vegas Sands Corp. Air Products and Chemicals Inc. Northern Trust Corp. Illinois Tool Works Inc. TravelCenters of America LLC

Exergoeconomic evaluation of single mixed refrigerant natural gas liquefaction processes

Exergy and exergoeconomic analysis is performed for single mixed refrigerant Linde and Air Products and Chemicals Inc, processes, which are among the most important and popular natural gas liquefaction processes. Cost of exergy destruction, exergoeconomic factor, exergy destruction and exergy efficiency are calculated. Results of exergy analysis demonstrates that exergy efficiency of Linde process is around 40.2%, and its total exergy destruction rate is 93,229kW. The exergy efficiency and exergy destruction rate for Air Products and Chemicals Inc, process are 45.0% and 72,245kW respectively. Results of exergoeconomic analysis suggests that maximum exergy destruction cost for Linde process is related to E-2 heat exchanger which is 34,072$/h and for Air Products and Chemicals Inc, process maximum exergy destruction cost is related to E-2 heat exchanger with the value of 4125kW. Sensitivity of cost of exergy destruction and exergoeconomic factor to operating variables of the processes are studied and analyzed.

Pharmacologic Stimulation of Cytochrome P450 46A1 and Cerebral Cholesterol Turnover in Mice

Cytochrome P450 46A1 (CYP46A1) is a brain-specific cholesterol 24-hydroxylase responsible for the majority of cholesterol elimination from the brain. Genetically increased CYP46A1 expression in mice leads to improved cognition and decreases manifestations of Alzheimer disease. We found that four pharmaceuticals (efavirenz (EFV), acetaminophen, mirtazapine, and galantamine) prescribed for indications unrelated to cholesterol maintenance increased CYP46A1 activity in vitro. We then evaluated the anti-HIV medication EFV for the mode of interaction with CYP46A1 and the effect on mice. We propose a model for CYP46A1 activation by EFV and show that EFV enhanced CYP46A1 activity and cerebral cholesterol turnover in animals with no effect on the levels of brain cholesterol. The doses of EFV administered to mice and required for the stimulation of their cerebral cholesterol turnover are a hundred times lower than those prescribed to HIV patients. At such small doses, EFV may be devoid of adverse effects elicited by high drug concentrations. CYP46A1 could be a novel therapeutic target and a tool to further investigate the physiological and medical significance of cerebral cholesterol turnover.

Ca2+-independent Binding of Anionic Phospholipids by Phospholipase C δ1 EF-hand Domain

Recombinant EF-hand domain of phospholipase C δ1 has a moderate affinity for anionic phospholipids in the absence of Ca(2+) that is driven by interactions of cationic and hydrophobic residues in the first EF-hand sequence. This region of PLC δ1 is missing in the crystal structure. The relative orientation of recombinant EF with respect to the bilayer, established with NMR methods, shows that the N-terminal helix of EF-1 is close to the membrane interface. Specific mutations of EF-1 residues in full-length PLC δ1 reduce enzyme activity but not because of disturbing partitioning of the protein onto vesicles. The reduction in enzymatic activity coupled with vesicle binding studies are consistent with a role for this domain in aiding substrate binding in the active site once the protein is transiently anchored at its target membrane.

Effectiveness of Endodontic Disinfecting Solutions against Young and Old Enterococcus faecalis Biofilms in Dentin Canals

IntroductionEnterococcus faecalis is a species commonly isolated from persistent root canal infections. The purpose of this study was to compare the antibacterial effects of different disinfecting solutions on young and old E. faecalis biofilms in dentin canals using a novel dentin infection model and confocal laser scanning microscopy (CLSM). MethodsThe bacteria were introduced into the dentinal tubules by centrifugation. After 1 day and 3 weeks of incubation, 40 infected dentin specimens were subjected to 1 and 3 minutes of exposure to disinfecting solutions, which included 2% sodium hypochlorite (NaOCl) (EMD Chemicals Inc, Darmstadt, Germany), 6% NaOCl, 2% chlorhexidine (CHX) (Sigma Chemical Co, St Louis, MO), and QMiX (Dentsply Tulsa Dental, Tulsa, OK). The proportions of dead and live bacteria inside the dentinal tubules after exposure to these disinfectants were assessed by CLSM using a LIVE/DEAD bacterial viability stain. ResultsSignificantly fewer bacteria were killed in the 3-week-old dentin biofilm than in the 1-day-old biofilm. Three minutes of exposure resulted in more dead bacteria than 1 minute of exposure for both biofilms in all experimental groups (P < .05). Six percent NaOCl and QMiX were the most effective disinfecting solutions against the young biofilm, whereas against the 3-week-old biofilm, 6% NaOCl was the most effective followed by QMiX. Two percent NaOCl was equally effective as 2% CHX. All the disinfecting agents killed significantly more bacteria than the sterile water used as a negative control (P < .05). ConclusionsWithin dentin canals, bacteria in established biofilms are less easily killed by endodontic medicaments than bacteria in young biofilms.

Crystal Structure of the E2 Domain of Amyloid Precursor Protein-like Protein 1 in Complex with Sucrose Octasulfate

Missense mutations in the amyloid precursor protein (APP) gene can cause familial Alzheimer disease. It is thought that APP and APP-like proteins (APLPs) may play a role in adhesion and signal transduction because their ectodomains interact with components of the extracellular matrix. Heparin binding induces dimerization of APP and APLPs. To help explain how these proteins interact with heparin, we have determined the crystal structure of the E2 domain of APLP1 in complex with sucrose octasulfate (SOS). A total of three SOS molecules are bound to the E2 dimer. Two SOSs are bound inside a narrow intersubdomain groove, and the third SOS is bound near the two-fold axis of the protein. Mutational analyses show that most residues interacting with SOS also contribute to heparin binding, although in varying degrees; a deep pocket, defined by His-376, Lys-422, and Arg-429, and an interfacial site between Lys-314 and its symmetry mate are most important in the binding of the negatively charged polysaccharide. Comparison with a lower resolution APP structure shows that all key heparin binding residues are conserved and identically positioned, suggesting that APLP1 and APP may bind heparin similarly. In transfected HEK-293 cells, mutating residues responsible for heparin binding causes little change in the proteolysis of APP by the secretases. However, mutating a pair of conserved basic residues (equivalent to Arg-414 and Arg-415 of APLP1) immediately adjacent to the heparin binding site affects both the maturation and the processing of APP.

Tgfβ Signaling Directly Induces Arf Promoter Remodeling by a Mechanism Involving Smads 2/3 and p38 MAPK

We have investigated how the Arf gene product, p19(Arf), is activated by Tgfβ during mouse embryo development to better understand how this important tumor suppressor is controlled. Taking advantage of new mouse models, we provide genetic evidence that Arf lies downstream of Tgfβ signaling in cells arising from the Wnt1-expressing neural crest and that the anti-proliferative effects of Tgfβ depend on Arf in vivo. Tgfβ1, -2, and -3 (but not BMP-2, another member of the Tgfβ superfamily) induce p19(Arf) expression in wild type mouse embryo fibroblasts (MEFs), and they enhance Arf promoter activity in Arf(lacZ/lacZ) MEFs. Application of chemical inhibitors of Smad-dependent and -independent pathways show that SB431542, a Tgfβ type I receptor (TβrI) inhibitor, and SB203580, a p38 MAPK inhibitor, impede Tgfβ2 induction of Arf. Genetic studies confirm the findings; transient knockdown of Smad2, Smad3, or p38 MAPK blunt Tgfβ2 effects, as does Cre recombinase treatment of Tgfbr2(fl/fl) MEFs to delete Tgfβ receptor II. Chromatin immunoprecipitation reveals that Tgfβ rapidly induces Smads 2/3 binding and histone H3 acetylation at genomic DNA proximal to Arf exon 1β. This is followed by increased RNA polymerase II binding and progressively increased Arf primary and mature transcripts from 24 through 72 h, indicating that increased transcription contributes to p19(Arf) increase. Last, Arf induction by oncogenic Ras depends on p38 MAPK but is independent of TβrI activation of Smad 2. These findings add to our understanding of how developmental and tumorigenic signals control Arf expression in vivo and in cultured MEFs.

Structural and Functional Characterization of the C-terminal Transmembrane Region of NBCe1-A

NBCe1-A and AE1 both belong to the SLC4 HCO(3)(-) transporter family. The two transporters share 40% sequence homology in the C-terminal transmembrane region. In this study, we performed extensive substituted cysteine-scanning mutagenesis analysis of the C-terminal region of NBCe1-A covering amino acids Ala(800)-Lys(967). Location of the introduced cysteines was determined by whole cell labeling with a membrane-permeant biotin maleimide and a membrane-impermeant 2-((5(6)-tetramethylrhodamine)carboxylamino) ethyl methanethiosulfonate (MTS-TAMRA) cysteine-reactive reagent. The results show that the extracellular surface of the NBCe1-A C-terminal transmembrane region is minimally exposed to aqueous media with Met(858) accessible to both biotin maleimide and TAMRA and Thr(926)-Ala(929) only to TAMRA labeling. The intracellular surface contains a highly exposed (Met(813)-Gly(828)) region and a cryptic (Met(887)-Arg(904)) connecting loop. The lipid/aqueous interface of the last transmembrane segment is at Asp(960). Our data clearly determined that the C terminus of NBCe1-A contains 5 transmembrane segments with greater average size compared with AE1. Functional assays revealed only two residues in the region of Pro(868)-Leu(967) (a functionally important region in AE1) that are highly sensitive to cysteine substitution. Our findings suggest that the C-terminal transmembrane region of NBCe1-A is tightly folded with unique structural and functional features that differ from AE1.

Regulation of Proline-rich Akt Substrate of 40 kDa (PRAS40) Function by Mammalian Target of Rapamycin Complex 1 (mTORC1)-mediated Phosphorylation

The rapamycin-sensitive mammalian target of rapamycin (mTOR) complex 1 (mTORC1) contains mTOR, raptor, mLST8, and PRAS40 (proline-rich Akt substrate of 40 kDa). PRAS40 functions as a negative regulator when bound to mTORC1, and it dissociates from mTORC1 in response to insulin. PRAS40 has been demonstrated to be a substrate of mTORC1, and one phosphorylation site, Ser-183, has been identified. In this study, we used two-dimensional phosphopeptide mapping in conjunction with mutational analysis to show that in addition to Ser-183, mTORC1 also phosphorylates Ser-212 and Ser-221 in PRAS40 when assayed in vitro. Mutation of all three residues to Ala markedly reduces mTORC1-mediated phosphorylation of PRAS40 in vitro. All three sites were confirmed to be phosphorylated in vivo by [(32)P]orthophosphate labeling and peptide mapping. Phosphorylation of Ser-221 and Ser-183 but not Ser-212 is sensitive to rapamycin treatment. Furthermore, we demonstrate that mutation of Ser-221 to Ala reduces the interaction with 14-3-3 to the same extent as mutation of Thr-246, the Akt/protein kinase B-phosphorylated site. We also find that mutation of Ser-221 to Ala increases the inhibitory activity of PRAS40 toward mTORC1. We propose that after mTORC1 kinase activation by upstream regulators, PRAS40 is phosphorylated directly by mTOR, thus contributing to the relief of PRAS40-mediated substrate competition.

Identification and Molecular Cloning of a Novel Glycoside Hydrolase Family of Core 1 Type O-Glycan-specific Endo-α-N-acetylgalactosaminidase from Bifidobacterium longum

We found endo-alpha-N-acetylgalactosaminidase in most bifidobacterial strains, which are predominant bacteria in the human colon. This enzyme catalyzes the liberation of galactosyl beta1,3-N-acetyl-D-galactosamine (Galbeta1,3GalNAc) alpha-linked to serine or threonine residues from mucin-type glycoproteins. The gene (engBF) encoding the enzyme has been cloned from Bifidobacterium longum JCM 1217. The protein consisted of 1,966 amino acid residues, and the central domain (590-1381 amino acid residues) exhibited 31-53% identity to hypothetical proteins of several bacteria including Clostridium perfringens and Streptococcus pneumoniae. The recombinant protein expressed in Escherichia coli liberated Galbeta1,3GalNAc disaccharide from Galbeta1,3GalNAcalpha1pNP and asialofetuin, but did not release GalNAc, Galbeta1,3(GlcNAcbeta1,6)GalNAc, GlcNAcbeta1,3GalNAc, and Galbeta1,3GlcNAc from each p-nitrophenyl (pNP) substrate, and also did not release sialo-oligosaccharides from fetuin, indicating its strict substrate specificity for the Core 1-type structure. The stereochemical course of hydrolysis was determined by (1)H NMR and was found to be retention. Site-directed mutagenesis of a total of 22 conserved Asp and Glu residues suggested that Asp-682 and Asp-789 are critical residues for the catalytic activity of the enzyme. The enzyme also exhibited transglycosylation activity toward various mono- and disaccharides and 1-alkanols, demonstrating its potential to synthesize neoglycoconjugates. This is the first report for the isolation of a gene encoding endo-alpha-N-acetylgalactosaminidase from any organisms and for the establishment of a new glycoside hydrolase family (GH family 101).

A Salmonella typhimurium Effector Protein SifA Is Modified by Host Cell Prenylation and S-Acylation Machinery

SifA is a Salmonella effector protein that is required for maintenance of the vacuolar membrane that surrounds replicating bacteria. It associates with the Salmonella-containing vacuole but how it interacts with the membrane is unknown. Here we show by immunofluorescence, S100 fractionation and Triton X-114 partitioning that the membrane association and targeting properties of SifA are influenced by a motif encoded within the C-terminal six amino acids. This sequence shares homology with both CAAX and Rab geranylgeranyl transferase prenylation motifs. We characterized the post-translational processing of SifA and showed that the cysteine residue within the CAAX motif is modified by isoprenoid addition through the action of protein geranylgeranyl transferase I. SifA was additionally modified by S-acylation of an adjacent cysteine residue. Similar modifications to host cell proteins regulate numerous functions including protein targeting, membrane association, protein-protein interaction, and signal transduction. This is the only known example of a bacterial effector protein that is modified both by mammalian cell S-acylation and prenylation machinery.

Air Products &amp; Chemicals Inc.

Mergent's Dividend AchieversVolume 2, Issue 2 p. 4-4 U.S. Company Report Air Products & Chemicals Inc.† First published: 22 April 2005 https://doi.org/10.1002/div.2175 † Contact: : John P. Jones III — Chmn., Pres., C.E.O. Address: : 7201 Hamilton Boulevard, Allentown, PA 18195-1501 Web Site: : www.airproducts.com AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onFacebookTwitterLinkedInRedditWechat Abstract Chemicals (MIC: 11.1 SIC: 813 NAIC: 25120) Air Products & Chemicals is engaged in the business of industrial gas and related industrial process equipment and is a producer of certain chemicals. The gases business segment recovers and distributes industrial gases such as oxygen, nitrogen, helium, argon, and hydrogen, and a variety of medical and specialty gases, and also includes Co.'s healthcare business. The chemicals business segment produces and markets performance materials and chemical intermediates. The equipment business segment designs and manufactures equipment for cryogenic air separation, gas processing, natural gas liquefaction, and hydrogen purification. Volume2, Issue2Spring 2005Pages 4-4 RelatedInformation

Lyondell announces agreement to acquire Millennium Chemicals Inc.

Lyondell announces agreement to acquire Millennium Chemicals Inc.

Air Products to build, operate Swiss hydrogen plant

Air Products and Chemicals Inc has signed a long-term hydrogen supply agreement with Petroplus Refining Cressier SA to build, own and operate a 7 million standard-cubic-feet-per-day hydrogen facility for Petroplus’s Cressier, Switzerland refinery. Visit www.filtsep.com for the latest filtration industry news

Air Products to build, operate Swiss hydrogen plant

Air Products and Chemicals Inc has signed a long-term hydrogen supply agreement with Petroplus Refining Cressier SA to build, own and operate a 7 million standard-cubic-feet-per-day hydrogen facility for Petroplus’s Cressier, Switzerland refinery. Visit www.worldpumps.com for the latest pump industry news