DOCSLIB.ORG

Appendix a Acid-Base Calculations

Total Page：16

File Type：pdf, Size：1020Kb

Download full-text PDF Read full-text

Load more

Appendix A Acid-Base Calculations A. 1. IO NIC STRENGTH Ionic strength (/) is a measure of ion concentration, de­ and based on Eq. (1.2) fined by the equation (W] = (1.0 X 10-14)/0.040 = 2.5 X 10- 13 so that where c. is the concentration of ion i, z. is the charge of ' ion i, and L is "the sum ~f." pH = -log[W] = -log(2.5 X 10- 13) = 12.6 = 13 Problem: What is the ionic strength of a O.lM solu­ tion of (NH4 ) 2SO4 ? Solution: Each "molecule" of (NH4) 2SO4 yields two A.3. HE DERSON- H ASSE LBALCH NH; ions and one So~- ion. Hence, EQUATIO N [NHl l = c 1 = 0.2M; z1 = + 1 [So~ - ]= c2 = 0.1M; z2 = - 2 Problem 1: Calculate the pH of a solution made by mix­ 1 I = I/2 ~{ (0.2 X 12) + (0.1 X ( - 2)2]} = 0.3 ing 15.0mlof 1.00 X 10- MK2HP04 and25.0mlof2.00 2 X 10- MKH2P04 . Solution: Molar concentrations of the two salts in the A.2. pH final volume (15.0 + 25.0 = 40.0 ml) are: 1 forK2HP04 : 15.0 X (1.00 X 10- )/40.0 = 0.0375M Problem 1: What is the pH of 0.01 OM HCI, assuming that for KH2P04 : 25.0 X (2.00 X 10- 2)/40.0 = 0.01 25M the HCl is 100% ionized? Substituting these values into the Henderson- Hasselbalch Solution: equation and using pK~ = 7.21 yields [W] = O.OlOM = 1.0 X 10-2M pH = -log[W] = -log(l.O X 10- 2) = 2.0 (0.0375) pH = 7.21 +log (0.0125) = 7.69 Problem 2: What is the pH of 0.020M Ca(OH)2 , as­ suming that it is 100 % ionized? Problem 2: Given that lactic acid (HA = CH3 - Solution: Since each "molecule" of Ca(OH)2 yields CHOH -COOH; A- = CH3 -CHOH - coo- ) has a two OH- ions, pK~ of 3.86, calculate the percent of lactic acid present in 503 504 APPENDIX A its dissociated form (A-) at a pH that is one unit above its (0.400- x) = 0.065 mol ofK2HP04/liter pK~ (i.e., at pH 4.86). Solution: At pH 4.86, the Henderson-Hasselbalch Since you wish to prepare not I liter but only 500 ml, equation takes the form you will need one-half of the above number of moles, namely, 0.168 mol ofKH2P04 (22.8 g) and 0.033 mol of [A-] K2HP04 (5.75 g). To prepare the buffer, you would weigh 4.86 = 3.86 + log [HA] out these amounts, dissolve them in water, and dilute the solution to a final volume of 500 ml. Hence, Problem 2: How would you prepare 500 ml of a O.lOOM acetate buffer at pH 5.00 from acetic acid and NaOH? The pK~ of acetic acid is 4.76. Solution: Substituting into the Henderson-Hassel­ balch equation yields so that [A-] 5.00 = 4.76 + log[HA] [A-] = 10 = !.Q [HA] 1 Hence, For every mole of HA per liter, there exist 10 moles of A- per liter. The percentage of lactic acid present in the [A-] log [HA] = 0.24 A- form (percent dissociation) is [A-] [A-] 10 [HA] = 1.74 %A-= [A-]+ [HA] X 100 = (10 + 1) X 100 = 91% Since you wish to prepare a O.IOOM buffer, the total, In like manner you can calculate that, at a pH that is combined concentration of A- and HA must be 0.1 OOM, one unit below the pK~ value (pH= 2.86), 91% of the lac­ that is, tic acid will be present in its undissociated form (HA). You can also show that at a pH that is two units above (or be­ [A-] + [HA] = 0.100 low) the pK~ value, the percentage of lactic acid present in the dissociated (or undissociated) form rises to 99%. Each of the last two equations has two unknowns, [A-] and [HA]. You can solve two equations with two un­ knowns simultaneously. From the first equation, you have that Problem 1: How would you prepare 500 ml of a 0.400M [A-] = 1.74[HA] phosphate buffer at pH 6.50 from solid KH2PO 4 and ~HPO 4 ? The second pK~ of H3PO4 is 7.21. Substituting for [A-] into the second equation yields Solution: A 0.400M phosphate buffer contains a to­ tal of 0.400 mole of phosphate salts per liter. Hence, let­ 1.74[HA] + [HA] = 2.74[HA] = 0.100 ting x equal the number of moles of KH2PO 4 per liter, it follows that (0.400 - x) is the number of moles of so that K2HPO4 per liter. Substituting into the Henderson-Has­ [HA] = 0.0365M (0.0365 mol/liter) selbalch equation yields [A-] = 1.74[HA] = 0.0635M (0.0635 mol/liter) 6.50 = 7.21 +log (0.400- x) As you wish to prepare only 500 ml, not 1 liter, you X will need one-half of the above number of moles, name­ log (0.400- x) = -0.71 ly, 0.0182 mol of HA (acetic acid) and 0.0318 mol of A­ X (acetate). Since both buffer components are derived from acetic acid, you must start with 0.0500 mol of acetic acid (0.400- x) = 0.195 X and convert some of it to acetate by adding NaOH. From the neutralization reaction involved, x = 0.335 mol of KH2PO iliter APPENDIX A 505 0.0500- 0.0318 = 0.0182 mol you see that adding 1.0 mol of NaOH converts 1.0 mol of To sum up, you would prepare this buffer by obtain­ acetic acid to 1.0 mol of acetate. To produce 0.0318 mol ing 0.0500 mol of acetic acid (2.87 ml of concentrated of acetate, you must add 0.0318 mol of NaOH. After acetic acid, which is 17 .4M), adding 0.0318 mol of solid adding the NaOH, you will be left with the required NaOH (1.27 g), and diluting the mixture to 500 mi. amount of acetic acid: Appendix B Principles of Organic Chemistry TIONAL CR LITY Functional groups consist of two or more atoms and pos­ Many objects are asymmetric in their structure; they have sess characteristic structures and chemical reactivities. A a "handedness" like that of the left and right hands. If you given functional group generally behaves the same way in visualize your two hands placed on either side of a flat all molecules containing that group. Table B.l shows mirror, one hand will appear to be the mirror image of the some of the functional groups found in biomolecules. other. But the two hands are not identical. You cannot put one hand on top of the other, with both palms down. The two hands cannot be superimposed in space. B.., POL\ In much the same manner, biomolecules can have structural asymmetry, resulting in mirror images that Polar reactions result from the attractive force between cannot be superimposed in space. We use the term chi­ positive and negative charges (or partial charges) on mol­ rality ("handedness") to refer to the right- and left-hand­ ecules. We call the two reactants in a polar reaction nu­ edness of a molecule. At the molecular level, chirality cleophile and electrophile. A nucleophile consists of an arises when a compound contains one or more chiral atom or a group of atoms that has an electron-rich site and centers. A chiral center comprises either a chiral carbon forms a bond by donating a pair ofelectrons. By contrast, atom or some other asymmetric region in the molecule. an electrophile consists of an atom or a group of atoms A chiral carbon atom has four different substituents at­ that has an electron-poor site and forms a bond by ac­ tached to it (Figure B.l). Because tetravalent carbon is cepting a pair of electrons. We depict the electron-pair tetrahedral, these groups occupy the corners of a tetrahe­ movement by means of a curved arrow, using the con­ dron. Because of carbon's tetrahedral nature, the two vention that the electron pair moves from the tail to the mirror images of a chiral carbon cannot be superim­ head of the arrow: posed. Aside from carbon, several other atoms that form ........_ compounds having a tetrahedral structure (Si, N, P, S) can A:-- + s+ ---7 A:B exist as chiral centers under proper circumstances. Chiral Nucleophile Electrophile centers also result from molecular asymmetry that is not ----........_-- s+ s-:?" due to the presence of chiral atoms. The helical structures provide an example. A helix A:- + B: C ---7 A:B + of proteins and nucleic acids is intrinsically chiral; a left-handed helix constitutes a The second arrow in the second reaction indicates that nonidentical and nonsuperimposable mirror image of a C leaves, taking the two electrons of the B-C bond right-handed helix, much as a left-handed screw differs with it. from a right-handed screw. 507 508 APPENDIX B Table 8.1. Some Common Functional Groups in Biomolecules Compound type Structure Functional group I Alcohol R-C-OH Hydroxyl I ~0 Aldehyde R-C Carbonyl "R ~0 Ketone R-C Carbonyl Mirror "R· Figure B. l . The two enantiomers (mirror images) of a chiral carbon ~0 atom. Acid R- C Carboxyl "-oH I c is the concentration of the solution (in grams per 100 Amine R-C-N~ Amino ml). I The two mirror images of a compound containing a chiral carbon, called enantiomers, differ in their optical ~0 Amide R-C Amide rotation; they represent optical isomers.
Recommended publications
  • A Monitoring of Allantoin, Uric Acid, and Malondialdehyde Levels In

    A Monitoring of Allantoin, Uric Acid, and Malondialdehyde Levels In

    A Monitoring of Allantoin, Uric Acid, and Malondialdehyde Levels in Plasma and Erythrocytes after a 10-Minute Running Activity ROMAN KANĎÁR, XENIE ŠTRAMOVÁ, PETRA DRÁBKOVÁ, JANA KŘENKOVÁ Department of Biological and Biochemical Sciences, Faculty of Chemical Technology, University of Pardubice, Pardubice, Czech Republic A running title: Allantoin and Uric Acid Levels after Running Activity Correspondence to: Roman Kanďár, Ph.D., Department of Biological and Biochemical Sciences, Faculty of Chemical Technology, University of Pardubice, Studentska 573, 532 10 Pardubice, Czech Republic Tel.: +420 466037714 Fax: +420 466037068 E-mail: [email protected] Keywords: allantoin, uric acid, oxidative stress, antioxidants, short-term intense exercise 1 Summary Uric acid is the final product of human purine metabolism. It was pointed out that this compound acts as an antioxidant and is able to react with reactive oxygen species forming allantoin. Therefore, the measurement of allantoin levels may be used for the determination of oxidative stress in humans. The aim of the study was to clarify the antioxidant effect of uric acid during intense exercise. Whole blood samples were obtained from a group of healthy subjects. Allantoin, uric acid, and malondialdehyde levels in plasma and erythrocytes were measured using a HPLC with UV/Vis detection. Statistical significant differences in allantoin and uric acid levels during short-term intense exercise were found. Immediately after intense exercise, the plasma allantoin levels increased on the average of two hundred per cent in comparison to baseline. Plasma uric acid levels increased slowly, at an average of twenty per cent. On the other hand, there were no significant changes in plasma malondialdehyde.
  • Cutaneous Manifestations of Systemic Diseases 428 C2 Notes Dr

    Cutaneous Manifestations of Systemic Diseases 428 C2 Notes Dr

    Cutaneous Manifestations of systemic diseases 428 C2 Notes Dr. Eman Almukhadeb Cutaneous Manifestations of systemic diseases Dr. Eman Almukhadeb CUTANEOUS MANIFESTATIONS OF DIABETES MELLITUS: Specific manifestations: 1 Cutaneous Manifestations of systemic diseases 428 C2 Notes Dr. Eman Almukhadeb 1. Diabetes dermopathy or “SHIN SPOTS”: Most common cutaneous manifestation of diabetes; M > F, males over age 50 years with long standing diabetes. They are: bilateral, symmetrical, atrophic red-brownish macules and patches, over the shins mainly but can occur at any sites, asymptomatic. There is no effective treatment. 2. Necrobiosis Lipoidica Diabeticorum (NLD): Patients classically present with single or multiple red-brown papules, which progress to sharply demarcated yellow-brown atrophic, telangiectatic erythematic plaques with a violaceous, irregular border. Usually it’s unilateral. Common sites include shins followed by ankles, calves, thighs and feet. Very atrophic plaque so any trauma will lead to ulceration, it occurs in about 35% of cases. Cutaneous anesthesia, hypohidrosis and partial alopecia can be found Pathology: Palisading granulomas containing degenerating collagen. The nonenzymatic glycosylation of dermal collagen and elastin will lead to degeneration of the collagen and atrophy (necrobiosis). 2 Cutaneous Manifestations of systemic diseases 428 C2 Notes Dr. Eman Almukhadeb Approximately 60% of NLD patients have diabetes and 20% have glucose intolerance. Conversely, up to 3% of diabetics have NLD, so if a patient has NLD its common that he is diabetic, but not every diabetic patient have NLD. (Important) Women are more affected than men. Treatment: Ulcer prevention (by avoiding trauma). No impact of tight glucose control on likelihood of developing NLD. There are multiple treatment options available and all of them reported to be effective: o Intralesional steroids o Systemic aspirin: 300mg/day and dipyridamole: 75 mg/day.
  • A Theoretical Study of the Tryptophan Synthase Enzyme Reaction Network

    A Theoretical Study of the Tryptophan Synthase Enzyme Reaction Network

    A Theoretical Study of the Tryptophan Synthase Enzyme Reaction Network Dissertation zur Erlangung des akademischen Grades doctor rerum naturalium (Dr. rer. nat.) im Fach Chemie Spezialisierung: Physikalische und theoretische Chemie Eingereicht an der Mathematisch-Naturwissenschaftlichen Fakult¨at der Humboldt-Universit¨at zu Berlin von Dimitri Loutchko Pr¨asidentin der Humboldt-Universit¨atzu Berlin Prof. Dr.-Ing. Dr. Sabine Kunst Dekan der Mathematisch-Naturwissenschaftlichen Fakult¨at Prof. Dr. Elmar Kulke 1. Gutachter: Prof. Dr. Gerhard Ertl 2. Gutachter: Prof. Dr. Klaus Rademann 3. Gutachter: Prof. Dr. Yannick de Decker Tag der m¨undlichen Pr¨ufung:09.07.2018 ii Abstract iii Abstract The channeling enzyme tryptophan synthase provides a paradigmatic example of a chemical nanomachine. It catalyzes the biosynthesis of tryptophan from serine and indole glycerol phos- phate. As a single macromolecule, it possesses two distinct catalytic subunits and implements 13 different elementary reaction steps. A complex pattern of allosteric regulation is involved in its operation. The catalytic activity in a subunit is enhanced or inhibited depending on the state of the other subunit. The gates controlling arrival and release of the ligands can become open or closed depending on the chemical states. The intermediate product indole is directly channeled within the protein from one subunit to another, so that it is never released into the solution around it. In this thesis, the first single-molecule kinetic model of the enzyme is proposed and analyzed. All its transition rate constants are extracted from available experimental data, and thus, no fitting parameters are employed. Numerical simulations reveal strong correlations in the states of the active centers and the emergent synchronization of intramolecular processes in tryptophan synthase.
  • Allantoin-Hydrolyzed Animal Protein Product

    Allantoin-Hydrolyzed Animal Protein Product

    Patentamt JEuropaischesEuropean Patent Office ® Publication number: 0 087 374 Office européen des brevets B1 (Î2) EUROPEAN PATENT SPECIFICATION (45) Dateof publication of patent spécification: 27.05.87 ® Int. Cl.4: A 23 J 3/00, A 61 K 7/48 (§) Application number: 83400376.6 (22) Date of filing: 23.02.83 (54) Allantoin-hydrolyzed animal protein product. (30) Priority: 24.02.82 US 351722 (73) Proprietor: CHARLES OF THE RITZ GROUP LTD. 01.06.82 US 383404 40 West 57th Street 13.12.82 US 449117 New York, NY 10019 (US) (§) Dateof publication of application: (72) Inventor: Puchalski, Eugène 31.08.83 Bulletin 83/35 129 McAdoo Avenue Jersey City New Jersey (US) Inventor: Deckner, George E. (§) Publication of the grant of the patent: 645 Horst Street 27.05.87 Bulletin 87/22 Westfield New Jersey (US) Inventor: Dixon, Richard P. 23 Avondale Lane (§) Designated Contracting States: Aberdeen New Jersey (US) AT BE CH DE FR GB IT Ll LU NL SE Inventor: Donahue, Frances A. 2 Kimberley Court Apt. 16 Middletown New Jersey (US) (58) Références cited: FR-A-2510 563 Y- US-A-3 941722 (74) Représentative: Maiffret, Bernard et al Cû Law Offices of William J. Rezac 49, avenue SOAP, PERFUMERY AND COSMETICS, vol. 49, Franklin D. Roosevelt no. 11, November 1976, pages 481-485. S. B. F-75008 Paris (FR) ^ MECCA: "Uric acid, allantoin and allantoin ^ derivatives" SE1FEN- OLE - FETTE - WACHSE, vol. 97, no. 15, N 1971, pages 533-534. S. B. MECCA: "Neue 00 Allantoin-Derivate fur die kosmetische und O dermatologische Anwendung" C9 Note: Within nine months from the publication of t\the mention of the grant of the European patent, any person may give notice to the European Patent Office of opposopposition to the European patent granted.
  • Human Cellular Retinaldehyde-Binding Protein Has Secondary Thermal 9-Cis-Retinal Isomerase Activity

    Human Cellular Retinaldehyde-Binding Protein Has Secondary Thermal 9-Cis-Retinal Isomerase Activity

    See discussions, stats, and author profiles for this publication at: https://www.researchgate.net/publication/259313787 Human Cellular Retinaldehyde-Binding Protein Has Secondary Thermal 9-cis-Retinal Isomerase Activity Article in Journal of the American Chemical Society · January 2014 DOI: 10.1021/ja411366w · Source: PubMed CITATIONS READS 6 123 12 authors, including: Christin Bolze Rachel E. Helbling Vifor Pharma 13 PUBLICATIONS 21 CITATIONS 3 PUBLICATIONS 13 CITATIONS SEE PROFILE SEE PROFILE Arwen Pearson Guillaume Pompidor University of Hamburg European Molecular Biology Laboratory 78 PUBLICATIONS 1,083 CITATIONS 37 PUBLICATIONS 286 CITATIONS SEE PROFILE SEE PROFILE Some of the authors of this publication are also working on these related projects: Melanopsin View project AdPLA LRAT View project All content following this page was uploaded by Achim Stocker on 10 November 2017. The user has requested enhancement of the downloaded file. Article pubs.acs.org/JACS Human Cellular Retinaldehyde-Binding Protein Has Secondary Thermal 9-cis-Retinal Isomerase Activity † ‡ † § ∥ ⊥ ∇ Christin S. Bolze, , Rachel E. Helbling, Robin L. Owen, Arwen R. Pearson, Guillaume Pompidor, , ⊥ ⊥ ○ † # # Florian Dworkowski, Martin R. Fuchs, , Julien Furrer, Marcin Golczak, Krzysztof Palczewski, † † Michele Cascella,*, and Achim Stocker*, † ‡ Department of Chemistry and Biochemistry, and Graduate School for Cellular and Biomedical Sciences, University of Bern, Freiestrasse 3, 3012 Bern, Switzerland § Diamond Light Source, Harwell Science and Innovation Campus,
  • Shedding New Light on the Generation of the Visual Chromophore PERSPECTIVE Krzysztof Palczewskia,B,C,1 and Philip D

    Shedding New Light on the Generation of the Visual Chromophore PERSPECTIVE Krzysztof Palczewskia,B,C,1 and Philip D

    PERSPECTIVE Shedding new light on the generation of the visual chromophore PERSPECTIVE Krzysztof Palczewskia,b,c,1 and Philip D. Kiserb,d Edited by Jeremy Nathans, Johns Hopkins University School of Medicine, Baltimore, MD, and approved July 9, 2020 (received for review May 16, 2020) The visual phototransduction cascade begins with a cis–trans photoisomerization of a retinylidene chro- mophore associated with the visual pigments of rod and cone photoreceptors. Visual opsins release their all-trans-retinal chromophore following photoactivation, which necessitates the existence of pathways that produce 11-cis-retinal for continued formation of visual pigments and sustained vision. Proteins in the retinal pigment epithelium (RPE), a cell layer adjacent to the photoreceptor outer segments, form the well- established “dark” regeneration pathway known as the classical visual cycle. This pathway is sufficient to maintain continuous rod function and support cone photoreceptors as well although its throughput has to be augmented by additional mechanism(s) to maintain pigment levels in the face of high rates of photon capture. Recent studies indicate that the classical visual cycle works together with light-dependent pro- cesses in both the RPE and neural retina to ensure adequate 11-cis-retinal production under natural illu- minances that can span ten orders of magnitude. Further elucidation of the interplay between these complementary systems is fundamental to understanding how cone-mediated vision is sustained in vivo. Here, we describe recent
  • A New Insight Into Role of Phosphoketolase Pathway in Synechocystis Sp

    A New Insight Into Role of Phosphoketolase Pathway in Synechocystis Sp

    www.nature.com/scientificreports OPEN A new insight into role of phosphoketolase pathway in Synechocystis sp. PCC 6803 Anushree Bachhar & Jiri Jablonsky* Phosphoketolase (PKET) pathway is predominant in cyanobacteria (around 98%) but current opinion is that it is virtually inactive under autotrophic ambient CO2 condition (AC-auto). This creates an evolutionary paradox due to the existence of PKET pathway in obligatory photoautotrophs. We aim to answer the paradox with the aid of bioinformatic analysis along with metabolic, transcriptomic, fuxomic and mutant data integrated into a multi-level kinetic model. We discussed the problems linked to neglected isozyme, pket2 (sll0529) and inconsistencies towards the explanation of residual fux via PKET pathway in the case of silenced pket1 (slr0453) in Synechocystis sp. PCC 6803. Our in silico analysis showed: (1) 17% fux reduction via RuBisCO for Δpket1 under AC-auto, (2) 11.2–14.3% growth decrease for Δpket2 in turbulent AC-auto, and (3) fux via PKET pathway reaching up to 252% of the fux via phosphoglycerate mutase under AC-auto. All results imply that PKET pathway plays a crucial role under AC-auto by mitigating the decarboxylation occurring in OPP pathway and conversion of pyruvate to acetyl CoA linked to EMP glycolysis under the carbon scarce environment. Finally, our model predicted that PKETs have low afnity to S7P as a substrate. Metabolic engineering of cyanobacteria provides many options for producing valuable compounds, e.g., acetone from Synechococcus elongatus PCC 79421 and butanol from Synechocystis sp. strain PCC 68032. However, certain metabolites or overproduction of intermediates can be lethal. Tere is also a possibility that required mutation(s) might be unstable or the target bacterium may even be able to maintain the fux distribution for optimal growth balance due to redundancies in the metabolic network, such as alternative pathways.
  • CHEM 461 to CHEM 462 Mod 2013-10-16

    CHEM 461 to CHEM 462 Mod 2013-10-16

    CALIFORNIA STATE UNIVERSITY CHANNEL ISLANDS COURSE MODIFICATION PROPOSAL Courses must be submitted by October 15, 2013, and finalized by the end of the fall semester to make the next catalog (2014-15) production DATE (CHANGE DATE EACH TIME REVISED): 10/14/2013; REV 11.13.13 PROGRAM AREA(S) : CHEM Directions: All of sections of this form must be completed for course modifications. Use YELLOWED areas to enter data. All documents are stand alone sources of course information. 1. Indicate Changes and Justification for Each. [Mark an X by all change areas that apply then please follow-up your X’s with justification(s) for each marked item. Be as brief as possible but, use as much space as necessary.] x Course title Course Content Prefix/suffix Course Learning Outcomes x Course number References x Units GE Staffing formula and enrollment limits Other x Prerequisites/Corequisites Reactivate Course x Catalog description Mode of Instruction Justification: Modified CHEM 462 has a new number, since 461 will become Biochemistry I lab. CHEM 462 will also separate classroom and lab component, allowing for greater flexibility on the part of the students. Classroom and laboratory content for the modified CHEM 462. And the new lab class, CHEM 463, will consist of the same lab content as the original CHEM 461. Removes the pre-requisite course CHEM 305, Computer applications in Chemistry, as unnecessary for CHEM 462. Catalog description altered to remove reference to lab fee. 2. Course Information. [Follow accepted catalog format.] (Add additional prefixes
  • Analysis of Porcine Adipose Tissue Transcriptome Reveals Differences In

    Analysis of Porcine Adipose Tissue Transcriptome Reveals Differences In

    Analysis of porcine adipose tissue transcriptome reveals differences in de novo fatty acid synthesis in pigs with divergent muscle fatty acid composition Jordi Corominas, Yuliaxis Ramayo-Caldas, Anna Puig-Oliveras, Jordi Estelle Fabrellas, Anna Castello, Estefania Alves, Ramona N. Pena, Maria Ballester, Josep M. Folch To cite this version: Jordi Corominas, Yuliaxis Ramayo-Caldas, Anna Puig-Oliveras, Jordi Estelle Fabrellas, Anna Castello, et al.. Analysis of porcine adipose tissue transcriptome reveals differences in de novo fatty acid synthesis in pigs with divergent muscle fatty acid composition. BMC Genomics, BioMed Central, 2013, 14, 10.1186/1471-2164-14-843. hal-01193819 HAL Id: hal-01193819 https://hal.archives-ouvertes.fr/hal-01193819 Submitted on 29 May 2020 HAL is a multi-disciplinary open access L’archive ouverte pluridisciplinaire HAL, est archive for the deposit and dissemination of sci- destinée au dépôt et à la diffusion de documents entific research documents, whether they are pub- scientifiques de niveau recherche, publiés ou non, lished or not. The documents may come from émanant des établissements d’enseignement et de teaching and research institutions in France or recherche français ou étrangers, des laboratoires abroad, or from public or private research centers. publics ou privés. Corominas et al. BMC Genomics 2013, 14:843 http://www.biomedcentral.com/1471-2164/14/843 RESEARCH ARTICLE Open Access Analysis of porcine adipose tissue transcriptome reveals differences in de novo fatty acid synthesis in pigs with divergent muscle fatty acid composition Jordi Corominas1,2*, Yuliaxis Ramayo-Caldas1,2, Anna Puig-Oliveras1,2, Jordi Estellé3,4,5, Anna Castelló1, Estefania Alves6, Ramona N Pena7, Maria Ballester1,2 and Josep M Folch1,2 Abstract Background: In pigs, adipose tissue is one of the principal organs involved in the regulation of lipid metabolism.
  • Sterile Spikelets Assimilate Carbon in Sorghum and Related Grasses

    Sterile Spikelets Assimilate Carbon in Sorghum and Related Grasses

    bioRxiv preprint doi: https://doi.org/10.1101/396473; this version posted January 5, 2019. The copyright holder for this preprint (which was not certified by peer review) is the author/funder. This article is a US Government work. It is not subject to copyright under 17 USC 105 and is also made available for use under a CC0 license. 1 Sterile spikelets assimilate carbon in sorghum and related grasses Taylor AuBuchon-Elder1,a, Viktoriya Coneva1,a,d, David M. Goad a,b, Doug K. Allen2,a,c,e, and Elizabeth A. Kellogg2,a,e aDonald Danforth Plant Science Center, St. Louis, Missouri, 63132 USA bDepartment of Biology, Washington University, St. Louis, Missouri, 63130 USA cUSDA-ARS, St. Louis, Missouri, 63132 USA 1These authors contributed equally to this work. 2These authors contributed equally to this work. dCurrent address: Kenyon College, Gambier, OH 43022 eAddress correspondence to: [email protected]; [email protected] ORCID IDs: 0000-0002-0640-5135 (V.C.); 0000-0001-8658-6660 (D.M.G.); 0000-0001-8599- 8946 (D.K.A.); 0000-0003-1671-7447 (E.A.K.) Short title: Carbon assimilation in sorghum spikelets The author responsible for distribution of materials integral to the findings presented in this article is Elizabeth A. Kellogg ([email protected]). bioRxiv preprint doi: https://doi.org/10.1101/396473; this version posted January 5, 2019. The copyright holder for this preprint (which was not certified by peer review) is the author/funder. This article is a US Government work. It is not subject to copyright under 17 USC 105 and is also made available for use under a CC0 license.
  • The Use of Animal Models in Diabetes Research

    The Use of Animal Models in Diabetes Research

    Journal of Analytical & Pharmaceutical Research A Comprehensive Review: The Use of Animal Models in Diabetes Research Abstract Review Article Diabetes, a lifelong disease for which there is no cure yet. It is caused by reduced Volume 3 Issue 5 - 2016 production of insulin, or by decreased ability to use insulin. With high prevalence of diabetes worldwide, the disease constitutes a major health concern. Presently, it is an incurable metabolic disorder which affects about 2.8% of the global Iksula Services Pvt. Ltd, India population. Fifty percent of all people with Type I diabetes are under the age of 20. Insulin-dependent diabetes accounts for 3% of all new cases of diabetes *Corresponding author: Reena Rodrigues, Iksula Services each year. Hence, the search for compounds with novel properties to deal Pvt. Ltd, Mumbai, Maharashtra, India, Tel: 022-25924504; with this disease condition is still in progress. Due to time constrains, the use Email: of experimental models for the disease gives the necessary faster. The current review has attempted to bring together all the reported models, highlighted their Received: November 14, 2016 | Published: December 12, short comings and drew the precautions required for each technique. In Type 1 2016 or Diabetes mellitus, the body is unable to store and use glucose as an energy source effectively. Type 2 or diabetes insipidus is a heterogeneous disorder. In this review article we shall bring light as to how hyperglycemia, glucosuria and hyperlipidemia play an important role in the onset of diabetes. Keywords: Diabetes mellitus; Hyperglycemia; Diabetes insipidus; insulin Abbreviations: STZ: Streptozotocin; DNA: Deoxyribonucleic Acid; NAD: Nicotinamide Adenine Dinucleotide; GTG: Gold research.
  • Identifying Nucleic Acid-Associated Proteins in Mycobacterium Smegmatis by Mass Spectrometry-Based Proteomics Nastassja L

    Identifying Nucleic Acid-Associated Proteins in Mycobacterium Smegmatis by Mass Spectrometry-Based Proteomics Nastassja L

    Kriel et al. BMC Molecular and Cell Biology (2020) 21:19 BMC Molecular and https://doi.org/10.1186/s12860-020-00261-6 Cell Biology RESEARCH ARTICLE Open Access Identifying nucleic acid-associated proteins in Mycobacterium smegmatis by mass spectrometry-based proteomics Nastassja L. Kriel1*, Tiaan Heunis1,2, Samantha L. Sampson1, Nico C. Gey van Pittius1, Monique J. Williams1,3† and Robin M. Warren1† Abstract Background: Transcriptional responses required to maintain cellular homeostasis or to adapt to environmental stress, is in part mediated by several nucleic-acid associated proteins. In this study, we sought to establish an affinity purification-mass spectrometry (AP-MS) approach that would enable the collective identification of nucleic acid- associated proteins in mycobacteria. We hypothesized that targeting the RNA polymerase complex through affinity purification would allow for the identification of RNA- and DNA-associated proteins that not only maintain the bacterial chromosome but also enable transcription and translation. Results: AP-MS analysis of the RNA polymerase β-subunit cross-linked to nucleic acids identified 275 putative nucleic acid-associated proteins in the model organism Mycobacterium smegmatis under standard culturing conditions. The AP-MS approach successfully identified proteins that are known to make up the RNA polymerase complex, as well as several other known RNA polymerase complex-associated proteins such as a DNA polymerase, sigma factors, transcriptional regulators, and helicases. Gene ontology enrichment analysis of the identified proteins revealed that this approach selected for proteins with GO terms associated with nucleic acids and cellular metabolism. Importantly, we identified several proteins of unknown function not previously known to be associated with nucleic acids.