Photorespiration Pathways in a Chemolithoautotroph
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Intelligent Design, Abiogenesis, and Learning from History: Dennis R
Author Exchange Intelligent Design, Abiogenesis, and Learning from History: Dennis R. Venema A Reply to Meyer Dennis R. Venema Weizsäcker’s book The World View of Physics is still keeping me very busy. It has again brought home to me quite clearly how wrong it is to use God as a stop-gap for the incompleteness of our knowledge. If in fact the frontiers of knowledge are being pushed back (and that is bound to be the case), then God is being pushed back with them, and is therefore continually in retreat. We are to find God in what we know, not in what we don’t know; God wants us to realize his presence, not in unsolved problems but in those that are solved. Dietrich Bonhoeffer1 am thankful for this opportunity to nature, is the result of intelligence. More- reply to Stephen Meyer’s criticisms over, this assertion is proffered as the I 2 of my review of his book Signature logical basis for inferring design for the in the Cell (hereafter Signature). Meyer’s origin of biological information: if infor- critiques of my review fall into two gen- mation only ever arises from intelli- eral categories. First, he claims I mistook gence, then the mere presence of Signature for an argument against bio- information demonstrates design. A few logical evolution, rendering several of examples from Signature make the point my arguments superfluous. Secondly, easily: Meyer asserts that I have failed to refute … historical scientists can show that his thesis by not providing a “causally a presently acting cause must have adequate alternative explanation” for the been present in the past because the origin of life in that the few relevant cri- proposed candidate is the only known tiques I do provide are “deeply flawed.” cause of the effect in question. -
Proteomic Analysis of Mycelial Proteins from Magnaporthe Oryzae Under Nitrogen Starvation
Proteomic analysis of mycelial proteins from Magnaporthe oryzae under nitrogen starvation X.-G. Zhou1,2, P. Yu 2, C. Dong2, C.-X. Yao2, Y.-M. Ding2, N. Tao2 and Z.-W. Zhao1 1State Key Laboratory for Conservation and Utilization of Bio-Resources in Yunnan, Yunnan University, Kunming, China 2Key Laboratory of Southwestern Crop Gene Resources and Germplasm Innovation, Ministry of Agriculture and Yunnan Provincial Key Laboratory of Agricultural Biotechnology, Biotechnology and Germplasm Resources Institute, Yunnan Academy of Agricultural Sciences, Kunming, China Corresponding author: Z.W. Zhao E-mail: [email protected] Genet. Mol. Res. 15 (2): gmr.15028637 Received March 23, 2016 Accepted April 11, 2016 Published May 13, 2016 DOI http://dx.doi.org/10.4238/gmr.15028637 ABSTRACT. Magnaporthe oryzae is an important model system in studies of plant pathogenic fungi, and nitrogen is a key nutrient source affecting microbial growth and development. In order to understand how nitrogen stress causes changes in mycelial proteins, we analyzed differentially expressed mycelial proteins from the M. oryzae virulent strain CH-63 using two-dimensional electrophoresis and mass spectrometry in complete medium or under nitrogen starvation conditions. A total of 975 ± 70 and 1169 ± 90 protein spots were detected in complete medium and under nitrogen starvation conditions, respectively. Forty-nine protein spots exhibited at least 2-fold up- regulation or down-regulation at the protein level according to PDQuest7.4. Moreover, 43 protein spots were successfully identified by matrix-assisted laser desorption/ionization-time-of-flight/time-of-flight mass spectrometry. Among these spots, 6 proteins were functionally unknown and 37 proteins were categorized into 5 groups according to Genetics and Molecular Research 15 (2): gmr.15028637 ©FUNPEC-RP www.funpecrp.com.br X.-G. -
Lecture 29 Spring 2007
Geol. 656 Isotope Geochemistry Lecture 29 Spring 2007 ISOTOPE FRACTIONATION IN THE BIOSPHERE INTRODUCTION As we noted, biological processes often involve large isotopic fractionations. Indeed, biological proc- esses are the most important cause of variations in the isotope composition of carbon, nitrogen, and sul- fur. For the most part, the largest fractionations occur during the initial production of organic matter by the so-called primary producers, or autotrophs. These include all plants and many kinds of bacteria. The most important means of production of organic matter is photosynthesis, but organic matter may also be produced by chemosynthesis, for example at mid-ocean ridge hydrothermal vents. Large frac- tions of both carbon and nitrogen occur during primary production. Additional fractionations also oc- cur in subsequent reactions and up through the food chain as hetrotrophs consume primary producers, but these are generally smaller. CARBON ISOTOPE FRACTIONATION DURING PHOTOSYNTHESIS The most important of process producing isotopic fractionation of carbon is photosynthesis. As we earlier noted, photosynthetic fractionation of carbon isotopes is primarily kinetic. The early work of Park and Epstein (1960) suggested fractionation occurred in several steps. Subsequent work has eluci- dated the fractionations involved in these steps, which we will consider in more detail here. For terrestrial plants (those utilizing atmospheric CO2), the first step is diffusion of CO2 into the boundary layer surrounding the leaf, through the stomata, and internally in the leaf. The average δ13C of various species of plants has been correlated with the stomatal conductance (Delucia et al., 1988), in- dicating that diffusion into the plant is indeed important in fractionating carbon isotopes. -
Oxdc Antibody Rabbit Polyclonal Antibody Catalog # ABV11223
10320 Camino Santa Fe, Suite G San Diego, CA 92121 Tel: 858.875.1900 Fax: 858.622.0609 OxdC Antibody Rabbit Polyclonal Antibody Catalog # ABV11223 Specification OxdC Antibody - Product Information Application WB Primary Accession O34714 Reactivity Human Host Rabbit Clonality Polyclonal Isotype Rabbit IgG Calculated MW 43566 OxdC Antibody - Additional Information Gene ID 938620 Positive Control Western Blot: Recombinant protein Application & Usage Western blot: 1-4 Western blot of Oxalate decarboxylase µg/ml. antibody. Lane 1: rb- Oxalate decarboxylase - Other Names 10 ng. Lane 2: rb- Oxalate decarboxylase - 50 YvrK ng Target/Specificity OxdC OxdC Antibody - Background Antibody Form Oxalate decarboxylase (OxdC, EC4.1.1.2) is a Liquid manganese-containing enzyme, which decomposes oxalic acid and oxalate. With Appearance OxdC catalysis, oxalate is split into formate Colorless liquid and CO2. This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which Formulation 100 µg (0.5 mg/ml) of antibody in PBS pH cleave carbon-carbon bonds. The systematic 7.2 containing 0.01 % BSA, 0.01 % name of this enzyme class is oxalate thimerosal, and 50 % glycerol. carboxy-lyase (formate-forming). This enzyme is also called oxalate carboxy-lyase. The Handling enzyme is composed of two cupin domains, The antibody solution should be gently each of which contains a Mn (II) ion. This mixed before use. enzyme participates in glyoxylate and dicarboxylate metabolism. This enzyme has Reconstitution & Storage been recognized for diagnostics in diverse -20 °C biotechnological applications such as the clinical assay of oxalate in blood and urine, Background Descriptions therapeutics, process industry, and agriculture to lower oxalate levels in foods and the environment. -
Standard 2: CELL BIOLOGY – REVIEW of BASICS
Standard 2: CELL BIOLOGY – REVIEW OF BASICS CELL PART OR TYPE OF CELL WHERE FOUND WHAT DOES IT FUNCTION: MISCELLANEOUS ORGANELLE Prokaryotic cell Plant cell LOOK LIKE: Job it does in INFORMATION: things Eukaryotic cell Animal cell Describe or Draw the cell such as color, what it is Both Both made of, size, etc. plasma/cell See diagram Holds cell together Phospholipid bilayer with membrane both both Regulates what goes proteins in/out of cell Semipermeable cytoplasm both Clear thick jelly- Supports/protects both like material in cell cell organelles See diagram Control center nucleus eukaryotic both Contains DNA See diagram Where proteins are ribosome both both made See diagram Process proteins Golgi complex eukaryotic both that go to other /apparatus parts of cell Membrane-bound Digests materials lysosome eukaryotic animal sac of digestive within the cell enzymes Membrane-bound Stores water, food, One large one in plants vacuole eukaryotic both storage area waste and dissolved Many smaller ones in minerals animals endoplasmic Network of Transport materials Can be rough (with reticulum eukaryotic both membrane tubes throughout the cell ribosomes attached) or smooth (without ribosomes) See diagram Where cell respiration Called Powerhouse of cell mitochondria eukaryotic both occurs (releases Makes ATP from energy for cell to use) breaking down glucose See diagram Where photosynthesis Contains chlorophyll chloroplast eukaryotic plant takes place Converts light energy into chemical energy in glucose Some pro- and plant (also fungi Rigid structure -
Proteo-Metabolomic Investigation of Transgenic Rice Unravels Metabolic
www.nature.com/scientificreports OPEN Proteo-metabolomic investigation of transgenic rice unravels metabolic alterations and Received: 27 November 2018 Accepted: 24 June 2019 accumulation of novel proteins Published: xx xx xxxx potentially involved in defence against Rhizoctonia solani Subhasis Karmakar1, Karabi Datta1, Kutubuddin Ali Molla2,3, Dipak Gayen4, Kaushik Das1, Sailendra Nath Sarkar1 & Swapan K. Datta1 The generation of sheath blight (ShB)-resistant transgenic rice plants through the expression of Arabidopsis NPR1 gene is a signifcant development for research in the feld of biotic stress. However, to our knowledge, regulation of the proteomic and metabolic networks in the ShB-resistant transgenic rice plants has not been studied. In the present investigation, the relative proteome and metabolome profles of the non–transformed wild-type and the AtNPR1-transgenic rice lines prior to and subsequent to the R. solani infection were investigated. Total proteins from wild type and transgenic plants were investigated using two-dimensional gel electrophoresis (2-DE) followed by mass spectrometry (MS). The metabolomics study indicated an increased abundance of various metabolites, which draws parallels with the proteomic analysis. Furthermore, the proteome data was cross-examined using network analysis which identifed modules that were rich in known as well as novel immunity-related prognostic proteins, particularly the mitogen-activated protein kinase 6, probable protein phosphatase 2C1, probable trehalose-phosphate phosphatase 2 and heat shock protein. A novel protein, 14–3– 3GF14f was observed to be upregulated in the leaves of the transgenic rice plants after ShB infection, and the possible mechanistic role of this protein in ShB resistance may be investigated further. -
Lecture 7 - the Calvin Cycle and the Pentose Phosphate Pathway
Lecture 7 - The Calvin Cycle and the Pentose Phosphate Pathway Chem 454: Regulatory Mechanisms in Biochemistry University of Wisconsin-Eau Claire 1 Introduction The Calvin cycle Text The dark reactions of photosynthesis in green plants Reduces carbon from CO2 to hexose (C6H12O6) Requires ATP for free energy and NADPH as a reducing agent. 2 2 Introduction NADH versus Text NADPH 3 3 Introduction The Pentose Phosphate Pathway Used in all organisms Glucose is oxidized and decarboxylated to produce reduced NADPH Used for the synthesis and degradation of pentoses Shares reactions with the Calvin cycle 4 4 1. The Calvin Cycle Source of carbon is CO2 Text Takes place in the stroma of the chloroplasts Comprises three stages Fixation of CO2 by ribulose 1,5-bisphosphate to form two 3-phosphoglycerate molecules Reduction of 3-phosphoglycerate to produce hexose sugars Regeneration of ribulose 1,5-bisphosphate 5 5 1. Calvin Cycle Three stages 6 6 1.1 Stage I: Fixation Incorporation of CO2 into 3-phosphoglycerate 7 7 1.1 Stage I: Fixation Rubisco: Ribulose 1,5- bisphosphate carboxylase/ oxygenase 8 8 1.1 Stage I: Fixation Active site contains a divalent metal ion 9 9 1.2 Rubisco Oxygenase Activity Rubisco also catalyzes a wasteful oxygenase reaction: 10 10 1.3 State II: Formation of Hexoses Reactions similar to those of gluconeogenesis But they take place in the chloroplasts And use NADPH instead of NADH 11 11 1.3 State III: Regeneration of Ribulose 1,5-Bisphosphosphate Involves a sequence of transketolase and aldolase reactions. 12 12 1.3 State III: -
Introduction to the Cell Cell History Cell Structures and Functions
Introduction to the cell cell history cell structures and functions CK-12 Foundation December 16, 2009 CK-12 Foundation is a non-profit organization with a mission to reduce the cost of textbook materials for the K-12 market both in the U.S. and worldwide. Using an open-content, web-based collaborative model termed the “FlexBook,” CK-12 intends to pioneer the generation and distribution of high quality educational content that will serve both as core text as well as provide an adaptive environment for learning. Copyright ©2009 CK-12 Foundation This work is licensed under the Creative Commons Attribution-Share Alike 3.0 United States License. To view a copy of this license, visit http://creativecommons.org/licenses/by-sa/3.0/us/ or send a letter to Creative Commons, 171 Second Street, Suite 300, San Francisco, California, 94105, USA. Contents 1 Cell structure and function dec 16 5 1.1 Lesson 3.1: Introduction to Cells .................................. 5 3 www.ck12.org www.ck12.org 4 Chapter 1 Cell structure and function dec 16 1.1 Lesson 3.1: Introduction to Cells Lesson Objectives • Identify the scientists that first observed cells. • Outline the importance of microscopes in the discovery of cells. • Summarize what the cell theory proposes. • Identify the limitations on cell size. • Identify the four parts common to all cells. • Compare prokaryotic and eukaryotic cells. Introduction Knowing the make up of cells and how cells work is necessary to all of the biological sciences. Learning about the similarities and differences between cell types is particularly important to the fields of cell biology and molecular biology. -
Bioinorganic Chemistry Content
Bioinorganic Chemistry Content 1. What is bioinorganic chemistry? 2. Evolution of elements 3. Elements and molecules of life 4. Phylogeny 5. Metals in biochemistry 6. Ligands in biochemistry 7. Principals of coordination chemistry 8. Properties of bio molecules 9. Biochemistry of main group elements 10. Biochemistry of transition metals 11. Biochemistry of lanthanides and actinides 12. Modell complexes 13. Analytical methods in bioinorganic 14. Applications areas of bioinorganic chemistry "Simplicity is the ultimate sophistication" Leonardo Da Vinci Bioinorganic Chemistry Slide 1 Prof. Dr. Thomas Jüstel Literature • C. Elschenbroich, A. Salzer, Organometallchemie, 2. Auflage, Teubner, 1988 • S.J. Lippard, J.N. Berg, Bioinorganic Chemistry, Spektrum Akademischer Verlag, 1995 • J.E. Huheey, E. Keiter, R. Keiter, Anorganische Chemie – Prinzipien von Struktur und Reaktivität, 3. Auflage, Walter de Gruyter, 2003 • W. Kaim, B. Schwederski: Bioinorganic Chemistry, 4. Auflage, Vieweg-Teubner, 2005 • H. Rauchfuß, Chemische Evolution und der Ursprung des Lebens, Springer, 2005 • A.F. Hollemann, N. Wiberg, Lehrbuch der Anorganischen Chemie, 102. Auflage, de Gruyter, 2007 • I. Bertini, H.B. Gray, E.I. Stiefel, J.S. Valentine, Biological Chemistry, University Science Books, 2007 • N. Metzler-Nolte, U. Schatzschneier, Bioinorganic Chemistry: A Practical Course, Walter de Gruyter, 2009 • W. Ternes, Biochemie der Elemente, Springer, 2013 • D. Rabinovich, Bioinorganic Chemistry, Walter de Gruyter, 2020 Bioinorganic Chemistry Slide 2 Prof. Dr. Thomas Jüstel 1. What is Bioinorganic Chemistry? A Highly Interdisciplinary Science at the Verge of Biology, Chemistry, Physics, and Medicine Biochemistry Inorganic Chemistry (Micro)- Physics & Biology Spectroscopy Bioinorganic Chemistry Pharmacy & Medicine & Toxicology Physiology Diagnostics Bioinorganic Chemistry Slide 3 Prof. Dr. Thomas Jüstel 2. Evolution of the Elements Most Abundant Elements in the Universe According to Atomic Fraction Are: 1. -
Biochemistry Biotechnology Cell Biology
Undergraduate Biochemistry Opportunities www.ed.ac.uk/biology Biotechnology Cell Biology Biochem_Biotech_CellBio_A5.indd 1 21/05/2019 14:25 Biochemistry The programme combines coverage of the Biochemistry is the study of living systems at basic principles and knowledge underpinning the cellular and molecular level. This dynamic biotechnology and an appreciation of the field draws on a variety of subjects and has processes involved in converting an idea widespread application. Biochemistry applies a into a product. The objective is to provide a knowledge of chemistry and physical sciences firm foundation in molecular and microbial to investigate basic life processes. The subject biotechnology through compulsory sections has a major impact on modern medical research dealing with topics such as expression vectors, and upon the pharmaceutical, bioengineering, microbial fermentation, protein structure, drug agricultural and environmental industries. design and the development of antimicrobials and vaccines. The programme encourages the critical assessment of current developments in areas of Cell Biology biological interest. Modern cell biology is a dynamic discipline that combines the interests and techniques of many Biotechnology scientific fields. Cell biologists investigate the Biotechnology is concerned with industrial basic structural and functional units of life, the and biomedical applications of fundamental cells that compose all living organisms. They aim knowledge derived from biology. This covers to understand: cellular structure, composition many facets from making useful products and regulation, the organelles that cells contain, using microbial, plant or animal cells to using cell growth, nuclear and cellular division, and bioinformatics and structural biology to design cell death. Understanding how cells work is new drugs. Biotechnology is an exciting area fundamental to many areas of biology and is of with new developments each year in areas that particular importance to fields such as cancer affect us all. -
Independent Research Resources Demonstrations/Simulations
Independent Research Resources Independent Generation of Research (IGoR) - IGoR provides a platform for people to pool their knowledge, resources, time, and creativity so that everyone can pursue their own scientific curiosity. Virginia Junior Academy of Science Resource Library - Extensive collection of open-access resources for students in Biology & Medicine, Botany, Ecology, Environmental Sciences, Chemistry, Engineering and Physics The Society for Science and the Public Science Project Resources - A catalog of science resources that can support your quest to learn and do science Science Buddies - Ideas for science projects Teacher resources National Center for Science Education Scientist in the Classroom - Platform allows teachers to request classroom visits from scientists Genetics Education Outreach Network (GEON) - Network of genetics professionals HHMI BioInteractive Data Points - Explore and interpret primary data from published research Biotech in a Box Loan Kits - Shipped to your school from Fralin Life Sciences Institute at Virginia Tech Demonstrations/Simulations Genetic Science Learning Center- Simulations, videos and interactive activities that explore genetics, cell biology, neuroscience, ecology and health Remotely Accessible Instruments for Nanotechnology (RAIN) - Access and control nanoinstruments over the Internet in real-time with the assistance of an experienced engineer PhET Simulations - Interactive STEM simulations for all grade levels HHMI BioInteractive Interactive Media - Recommendations: Virus Explorer; Exploring -
Oxalate Decarboxylase from Bacillus Subtilis, Recombinant Cat
Oxalate Decarboxylase from Bacillus subtilis, recombinant Cat. No. NATE-1688 Lot. No. (See product label) Introduction Description Oxalate decarboxylase (OxdC, EC4.1.1.2) is a manganese-containing enzyme, which decomposes oxalic acid and oxalate. With OxdC catalysis, oxalate is split into formate and CO2. This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is oxalate carboxy-lyase (formate-forming). This enzyme is also called oxalate carboxy-lyase. The enzyme is composed of two cupin domains, each of which contains a Mn (II) ion. This enzyme participates in glyoxylate and dicarboxylate metabolism. This enzyme has been recognized for diagnostics in diverse biotechnological applications such as the clinical assay of oxalate in blood and urine, therapeutics, process industry, and agriculture to lower oxalate levels in foods and the environment. The recombinant protein made from the Bacillus Subtilis sequence includes OxdC with N-terminal His-tag. Synonyms Oxalate carboxy-lyase; EC 4.1.1.2; Oxalate decarboxylase; OxdC Product Information Species Bacillus subtilis Source E. coli Form Liquid Formulation In 50 mM NaOAC, pH 5.5. The activation was stopped by addition of 10 mM MMTS, which can be removed under reducing conditions. EC Number EC 4.1.1.2 CAS No. 9024-97-9 Molecular Weight 45.9 kDa Purity > 98% by SDS-PAGE Activity 150U/mg Creative Enzymes. All rights reserved. 45-1 Ramsey Road, Shirley, NY 11967, USA Tel:1-631-562-8517 1-516-512-3133 Fax:1-631-938-8127 E-mail: [email protected] http://www.creative-enzymes.com Concentration 2 mg/mL Unit Definition One unit is the amount of enzyme that generates 1.0 µmole of NADH at 37°C.