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Product Guide
www.megazyme.com es at dr hy o rb a C • s e t a r t s b u S e m y z n E • s e m y z n E • s t i K y a s s A Plant Cell Wall & Biofuels Product Guide 1 Megazyme Test Kits and Reagents Purity. Quality. Innovation. Barry V. McCleary, PhD, DScAgr Innovative test methods with exceptional technical support and customer service. The Megazyme Promise. Megazyme was founded in 1988 with the We demonstrate this through the services specific aim of developing and supplying we offer, above and beyond the products we innovative test kits and reagents for supply. We offer worldwide express delivery the cereals, food, feed and fermentation on all our shipments. In general, technical industries. There is a clear need for good, queries are answered within 48 hours. To validated methods for the measurement of make information immediately available to the polysaccharides and enzymes that affect our customers, we established a website in the quality of plant products from the farm 1994, and this is continually updated. Today, it gate to the final food. acts as the source of a wealth of information on Megazyme products, but also is the hub The commitment of Megazyme to “Setting of our commercial activities. It offers the New Standards in Test Technology” has been possibility to purchase and pay on-line, to continually recognised over the years, with view order history, to track shipments, and Megazyme and myself receiving a number many other features to support customer of business and scientific awards. -
(12) United States Patent (10) Patent No.: US 8,304,196 B2 Caprioli (45) Date of Patent: *Nov
USOO83 041.96B2 (12) United States Patent (10) Patent No.: US 8,304,196 B2 Caprioli (45) Date of Patent: *Nov. 6, 2012 (54) INSITUANALYSIS OF TISSUES 6,809,315 B2 10/2004 Ellson et al. .................. 250/288 7,534.338 B2 5/2009 Hafeman et al. ... 205/288 O O 2003.0049701 A1* 3, 2003 Muraca .......... 435/723 (75) Inventor: Richard Caprioli, Brentwood, TN (US) 2003/0186287 A1 10, 2003 Lin et al. 435/6 2004.0007673 A1* 1 2004 Coon et al. .. 250,424 (73) Assignee: Vanderbilt University, Nashville, TN 2007/0082356 A1 4/2007 Strom et al. ...................... 435/6 (US) FOREIGN PATENT DOCUMENTS (*) Notice: Subject to any disclaimer, the term of this WO WOO1,26460 4/2001 patent is extended or adjusted under 35 WO WOO3,O34024 4/2003 U.S.C. 154(b) by 0 days. OTHER PUBLICATIONS This patent is Subject to a terminal dis- Schwartz et al. (J. Mass Spectrometry 2003 vol. 38, p. 699-708).* claimer. Pauletti et al. (J. Clin. Oncology 2000 vol. 18, 3651-3664).* Office Action issued in U.S. Appl. No. 1 1/355.912, mailed Apr. 3, (21) Appl. No.: 12/942,840 2008. Office Action issued in U.S. Appl. No. 1 1/355.912, mailed Dec. 8, 1-1. 2009. (22) Filed: Nov. 9, 2010 Office Action issued in U.S. Appl. No. 1 1/355.912, mailed May 22, O O 2009. (65) Prior Publication Data Yanagisawa et al., “Proteomic patterns of tumour Subsets in non US 2011 FO190145 A1 Aug. 4, 2011 Small-cell lung cancer.” The Lancet, 362:433-439, 2003. -
Peraturan Badan Pengawas Obat Dan Makanan Nomor 28 Tahun 2019 Tentang Bahan Penolong Dalam Pengolahan Pangan
BADAN PENGAWAS OBAT DAN MAKANAN REPUBLIK INDONESIA PERATURAN BADAN PENGAWAS OBAT DAN MAKANAN NOMOR 28 TAHUN 2019 TENTANG BAHAN PENOLONG DALAM PENGOLAHAN PANGAN DENGAN RAHMAT TUHAN YANG MAHA ESA KEPALA BADAN PENGAWAS OBAT DAN MAKANAN, Menimbang : a. bahwa masyarakat perlu dilindungi dari penggunaan bahan penolong yang tidak memenuhi persyaratan kesehatan; b. bahwa pengaturan terhadap Bahan Penolong dalam Peraturan Kepala Badan Pengawas Obat dan Makanan Nomor 10 Tahun 2016 tentang Penggunaan Bahan Penolong Golongan Enzim dan Golongan Penjerap Enzim dalam Pengolahan Pangan dan Peraturan Kepala Badan Pengawas Obat dan Makanan Nomor 7 Tahun 2015 tentang Penggunaan Amonium Sulfat sebagai Bahan Penolong dalam Proses Pengolahan Nata de Coco sudah tidak sesuai dengan kebutuhan hukum serta perkembangan ilmu pengetahuan dan teknologi sehingga perlu diganti; c. bahwa berdasarkan pertimbangan sebagaimana dimaksud dalam huruf a dan huruf b, perlu menetapkan Peraturan Badan Pengawas Obat dan Makanan tentang Bahan Penolong dalam Pengolahan Pangan; -2- Mengingat : 1. Undang-Undang Nomor 18 Tahun 2012 tentang Pangan (Lembaran Negara Republik Indonesia Tahun 2012 Nomor 227, Tambahan Lembaran Negara Republik Indonesia Nomor 5360); 2. Peraturan Pemerintah Nomor 28 Tahun 2004 tentang Keamanan, Mutu dan Gizi Pangan (Lembaran Negara Republik Indonesia Tahun 2004 Nomor 107, Tambahan Lembaran Negara Republik Indonesia Nomor 4424); 3. Peraturan Presiden Nomor 80 Tahun 2017 tentang Badan Pengawas Obat dan Makanan (Lembaran Negara Republik Indonesia Tahun 2017 Nomor 180); 4. Peraturan Badan Pengawas Obat dan Makanan Nomor 12 Tahun 2018 tentang Organisasi dan Tata Kerja Unit Pelaksana Teknis di Lingkungan Badan Pengawas Obat dan Makanan (Berita Negara Republik Indonesia Tahun 2018 Nomor 784); MEMUTUSKAN: Menetapkan : PERATURAN BADAN PENGAWAS OBAT DAN MAKANAN TENTANG BAHAN PENOLONG DALAM PENGOLAHAN PANGAN. -
Function and Structure Studies of GH Family 31 and 97 \Alpha
110610 (RV-17) Biosci. Biotechnol. Biochem., 75 (12), 110610-1–9, 2011 Award Review Function and Structure Studies of GH Family 31 and 97 -Glycosidases Masayuki OKUYAMA Research Faculty of Agriculture, Hokkaido University, Kita-9, Nishi-9, Kita-ku, Sapporo 060-8589, Japan Online Publication, December 7, 2011 [doi:10.1271/bbb.110610] A huge number of glycoside hydrolases are classified an evolutionary relationship of proteins in the family, into the glycoside hydrolase family (GH family) based from which it is often possible to extract information on on their amino-acid sequence similarity. The glycoside function and structure.3) Classification in a GH family hydrolases acting on -glucosidic linkage are in GH has, accordingly, become indispensable for research on family 4, 13, 15, 31, 63, 97, and 122. This review deals glycoside hydrolases. Glycoside hydrolases are also mainly with findings on GH family 31 and 97 enzymes. divided into two mechanistic classes, inverting and Research on two GH family 31 enzymes is described: retaining enzymes: with inversion or net retention of clarification of the substrate recognition of Escherichia anomeric configuration during the catalytic reaction.4) coli -xylosidase, and glycosynthase derived from Schiz- The stereochemical outcome is generally conserved in a osaccharomyces pombe -glucosidase. GH family 97 is GH family. The inverting mechanism proceeds via a an aberrant GH family, containing inverting and simple single displacement. Two functional groups, retainingAdvance glycoside hydrolases. The inverting View enzyme usually carboxyl groups, act as general acid and general in GH family 97 displays significant similarity to base catalysts. The general acid catalyst donates a proton retaining -glycosidases, including GH family 97 retain- to the departure aglycon, and the general base catalyst ing -glycosidase, but the inverting enzyme has no simultaneously deprotonates the incoming water mole- catalytic nucleophile residue. -
Immunobiologicals Purified Proteins
Immunobiologicals i Cat. No. Enzyme Quantity PURIFIED PROTEINS 321731 Pullalanase, Crude Form 500 mg 835001 Superoxide Dismutase 25 mg 835002 100 mg Purified Enzymes 835011 Superoxide Dismutase 1 mg Cat. No. Enzyme Quantity 835012 5 mg 321241 β-N-Acetylhexosaminidase 0.5 U 321351 Thermolysin 250 mg 320941 N-Acetylmuramidase 10 mg 360941 Yeast LyticEnzyme,70,000u/mg 500mg 364841 Alkaline Phosphatase, Labeling Grade 5 KU 360942 1 g µ 360943 2 g 194966 Carboxypeptidase P, Excision Grade 20 g 360944 5 g 321271 Carboxypeptidase W 1 mg 360951 Yeast LyticEnzyme,5,000u/mg 5g 320961 Cellulase Y-C 10 g 360952 10 g 150 320301 Chondroitinase ABC Lyase, Protease Free 4x1 U 360953 25 g 320211 Chondroitinase ABC Lyase 4x5 U 360954 100 g Purified Proteins 320221 Chondroitinase AC-II Lyase 4x5 U 320921 Zymolyase 20T 1 g 320311 Chondroitinase AC-I 4x1 U 320932 Zymolyase 100T 250 mg 970551 Chondroitin Sulfate C 100 mg 320931 500 mg 970571 Chondroitin Sulfate D 10 mg 320231 Chondro-4-sulfatase 4x1.6 U 320241 Chondro-6-sulfatase 4x2.5 U 362001 Collagenase, Type 300C 300 KU Blood Proteins 321601 Dextranase 10 mg 321321 Endo-β-galactosidase 0.1 U ALBUMIN, BOVINE 321281 Endoglycosidase D 0.1 U Cat. No. Description Quantity 321282 0.5 U 810012 Crystalline 5 g 391311 Endoglycosidase H 0.2 U 810013 10 g 391312 2 U 810014 100 g 320182 Glucoamylase 2 KU 810032 Fraction V Powder, pH7.0 50 g 321291 Glycopeptidase A 1 mU 810033 100 g 321051 Glycosidases, Mixed 1 g 810034 500 g 321052 5 g 810035 1 kg 810036 5 kg 321001 Glycosidase 1 g 810532 Fraction V Powder, pH5.2 -
A Soluble Starch Synthase I Gene, Ibssi, Alters the Content, Composition, Granule Size and Structure of Starch in Transgenic
www.nature.com/scientificreports OPEN A soluble starch synthase I gene, IbSSI, alters the content, composition, granule size and Received: 23 January 2017 Accepted: 11 April 2017 structure of starch in transgenic Published: xx xx xxxx sweet potato Yannan Wang, Yan Li, Huan Zhang, Hong Zhai, Qingchang Liu & Shaozhen He Soluble starch synthase I (SSI) is a key enzyme in the biosynthesis of plant amylopectin. In this study, the gene named IbSSI, was cloned from sweet potato, an important starch crop. A high expression level of IbSSI was detected in the leaves and storage roots of the sweet potato. Its overexpression significantly increased the content and granule size of starch and the proportion of amylopectin by up- regulating starch biosynthetic genes in the transgenic plants compared with wild-type plants (WT) and RNA interference plants. The frequency of chains with degree of polymerization (DP) 5–8 decreased in the amylopectin fraction of starch, whereas the proportion of chains with DP 9–25 increased in the IbSSI-overexpressing plants compared with WT plants. Further analysis demonstrated that IbSSI was responsible for the synthesis of chains with DP ranging from 9 to 17, which represents a different chain length spectrum in vivo from its counterparts in rice and wheat. These findings suggest that theIbSSI gene plays important roles in determining the content, composition, granule size and structure of starch in sweet potato. This gene may be utilized to improve the content and quality of starch in sweet potato and other plants. In plants, starch consists of amylose and amylopectin. Amylose mainly comprises linear chains that are linked by α-1, 4 O-glycosidic bonds, whereas amylopectin is highly branched and contains 5–6% α-1,6 O-glycosidic bonds to generate glucan branches of various lengths1. -
Medical Bacteriology
LECTURE NOTES Degree and Diploma Programs For Environmental Health Students Medical Bacteriology Abilo Tadesse, Meseret Alem University of Gondar In collaboration with the Ethiopia Public Health Training Initiative, The Carter Center, the Ethiopia Ministry of Health, and the Ethiopia Ministry of Education September 2006 Funded under USAID Cooperative Agreement No. 663-A-00-00-0358-00. Produced in collaboration with the Ethiopia Public Health Training Initiative, The Carter Center, the Ethiopia Ministry of Health, and the Ethiopia Ministry of Education. Important Guidelines for Printing and Photocopying Limited permission is granted free of charge to print or photocopy all pages of this publication for educational, not-for-profit use by health care workers, students or faculty. All copies must retain all author credits and copyright notices included in the original document. Under no circumstances is it permissible to sell or distribute on a commercial basis, or to claim authorship of, copies of material reproduced from this publication. ©2006 by Abilo Tadesse, Meseret Alem All rights reserved. Except as expressly provided above, no part of this publication may be reproduced or transmitted in any form or by any means, electronic or mechanical, including photocopying, recording, or by any information storage and retrieval system, without written permission of the author or authors. This material is intended for educational use only by practicing health care workers or students and faculty in a health care field. PREFACE Text book on Medical Bacteriology for Medical Laboratory Technology students are not available as need, so this lecture note will alleviate the acute shortage of text books and reference materials on medical bacteriology. -
Characterization of Starch Debranching Enzymes of Maize Endosperm Afroza Rahman Iowa State University
Iowa State University Capstones, Theses and Retrospective Theses and Dissertations Dissertations 1998 Characterization of starch debranching enzymes of maize endosperm Afroza Rahman Iowa State University Follow this and additional works at: https://lib.dr.iastate.edu/rtd Part of the Biochemistry Commons, Molecular Biology Commons, and the Plant Sciences Commons Recommended Citation Rahman, Afroza, "Characterization of starch debranching enzymes of maize endosperm " (1998). Retrospective Theses and Dissertations. 12519. https://lib.dr.iastate.edu/rtd/12519 This Dissertation is brought to you for free and open access by the Iowa State University Capstones, Theses and Dissertations at Iowa State University Digital Repository. It has been accepted for inclusion in Retrospective Theses and Dissertations by an authorized administrator of Iowa State University Digital Repository. For more information, please contact [email protected]. INFORMATION TO USERS This manuscript has been reproduced from the microfilm master. UMI films the text directly from the original or copy submitted. Thus, some thesis and dissertation copies are in typewriter face, while others may be from any type of computer printer. The quality of this reproduction is dependent upon the quality of the copy submitted. Broken or indistinct print, colored or poor quality illustrations and photographs, print bleedthrough, substandard margins, and improper alignment can adversely affect reproduction. In the unlikely event that the author did not send UMI a complete manuscript and there are missing pages, these will be noted. Also, if unauthorized copyright material had to be removed, a note will indicate the deletion. Oversize materials (e.g., maps, drawings, charts) are reproduced by sectioning the original, beginning at the upper left-hand comer and continuing from left to right in equal sections with small overlaps. -
Understanding Starch Metabolism in Pea Seeds Towards Tailoring Functionality for Value-Added Utilization
International Journal of Molecular Sciences Review Understanding Starch Metabolism in Pea Seeds towards Tailoring Functionality for Value-Added Utilization Bianyun Yu 1,*, Daoquan Xiang 1 , Humaira Mahfuz 1,2, Nii Patterson 1 and Dengjin Bing 3 1 Aquatic and Crop Resource Development Research Centre, National Research Council Canada, 110 Gymnasium Place, Saskatoon, SK S7N 0W9, Canada; [email protected] (D.X.); [email protected] (H.M.); [email protected] (N.P.) 2 Department of Biology, Faculty of Science, University of Ottawa, 30 Marie Curie, Ottawa, ON K1N 6N5, Canada 3 Lacombe Research and Development Centre, Agriculture and Agri-Food Canada, 6000 C and E Trail, Lacombe, AB T4L 1W1, Canada; [email protected] * Correspondence: [email protected] Abstract: Starch is the most abundant storage carbohydrate and a major component in pea seeds, accounting for about 50% of dry seed weight. As a by-product of pea protein processing, current uses for pea starch are limited to low-value, commodity markets. The globally growing demand for pea protein poses a great challenge for the pea fractionation industry to develop new markets for starch valorization. However, there exist gaps in our understanding of the genetic mechanism underlying starch metabolism, and its relationship with physicochemical and functional properties, which is a prerequisite for targeted tailoring functionality and innovative applications of starch. This review Citation: Yu, B.; Xiang, D.; outlines the understanding of starch metabolism with a particular focus on peas and highlights Mahfuz, H.; Patterson, N.; Bing, D. the knowledge of pea starch granule structure and its relationship with functional properties, and Understanding Starch Metabolism in industrial applications. -
Xerox University Microfilms
INFORMATION TO USERS This material was produced from a microfilm copy of the original document. While the most advanced technological means to photograph and reproduce this document have been used, the quality is heavily dependent upon the quality of the original submitted. The following explanation of techniques is provided to help you understand markings or patterns which may appear on this reproduction. 1.The sign or "target" for pages apparently lacking from the document photographed is "Missing Page(s)". If it was possible to obtain the missing page(s) or section, they are spliced into the film along with adjacent pages. This may have necessitated cutting thru an image and duplicating adjacent pages to insure you complete continuity. 2. When an image on the film is obliterated with a large round black mark, it is an indication that the photographer suspected that the copy may have moved during exposure and thus cause a blurred image. You will find a good image of the page in the adjacent frame. 3. When a map, drawing or chart, etc., was part of the material being photographed the photographer followed a definite method in "sectioning" the material. It is customary to begin photoing at the upper left hand corner of a large sheet and to continue photoing from left to right in equal sections with a small overlap. If necessary, sectioning is continued again — beginning below the first row and continuing on until complete. 4. The majority of users indicate that the textual content is of greatest value, however, a somewhat higher quality reproduction could be made from "photographs" if essential to the understanding of the dissertation. -
STUDY of STARCH DEBRANCHING ENZYMES in DEVELOPING WHEAT KERNELS a Thesis Submitted to the College of Graduate Studies and Resear
STUDY OF STARCH DEBRANCHING ENZYMES IN DEVELOPING WHEAT KERNELS A Thesis Submitted to the College of Graduate Studies and Research in Partial Fulfilment of the Requirements for the Degree of Doctor of Philosophy in the Department of Biochemistry University of Saskatchewan Saskatoon By Supatcharee Netrphan Spring 2002 © Copyright Supatcharee Netrphan, 2002. All rights reserved. PERMISSION TO USE In presenting this thesis in partial fulfilment of the requirements for a Postgraduate degree from the University of Saskatchewan, I agree that the Libraries of this University may make it freely available for inspection. I further agree that permission for copying of this thesis in any manner, in whole or in part, for scholarly purposes may be granted by the professor or professors who supervised my thesis work or, in their absence, by the Head of the Department or the Dean of the College in which my thesis work was done. It is understood that any copying or publication or use of this thesis or parts thereof for financial gain shall not be allowed without my written permission. It is also understood that due recognition shall be given to me and to the University of Saskatchewan in any scholarly use which may be made of any material in my thesis. Requests for permission to copy or to make other use of material in this thesis in whole or in part should be addressed to: Head of the Department of Biochemistry University of Saskatchewan 107 Wiggins Road Saskatoon, Saskatchewan S7N 5E5 i ABSTRACT Starch debranching enzymes, which specifically hydrolyse a-1,6 glucosidic bonds in glucans containing both a-1,4 and a-1,6 linkages, are classified into two types: isoamylase (EC. -
Course Title: Systemic Bacteriology & Mycology
COURSE TITLE: BACTERIOLOGY COURSE CODE: MIPA-219 RECOMMENDED BOOKS 1. Essentials of Veterinary Microbiology (Fifth Edition) By G. R. Carter, M. M. Chengappa and C. A. W. Roberts 2. Veterinary Bacteriology and Virology By I. A .Merchant and R. A. Packer 3. Text Book of Veterinary Microbiology By S. N. Sharma and S. C. Adlakha 4. Pathogenesis of Bacterial Infections in Animals By C. L. Gyles and C. O. Thoen 5. Veterinary Microbiology and Microbial disease By P. J. Quinn, B. K. Markey, M. E. Carter, W. J. C. Donnelly, F. C. Leonard 6. Topley and Wilson‟s Microbiology and Microbial Infections (Volume-3; 9th Edition) By L. Collier, A. Balows and M.Sussman For Practical Class Purposes 1. Diagnostic Procedures in Veterinary Bacteriology and Mycology By G. R. Carter and J. R. Cole, Jr. 2. Color Atlas and Textbook of Diagnostic Microbiology (Fifth Edition) By Elmer W. Koneman et.al 1 BACTERIAL CLASSIFICATION AND NOMENCLATURE Systematic Bacteriology Systematic Bacteriology is a branch of Microbiology which embraces the classification and nomenclature of bacteria. Taxonomy Taxonomy is defined as the science of classification (orderly arrangement of organisms). Nomenclature Nomenclature is naming an organism by international rules according to its characteristics. Identification Identification refers - i. To isolate and distinguish desirable organisms from undesirable ones. ii. To verify the authenticity or special properties of a culture. Isolate An isolate is a pure culture derived from a heterogenous, wild population of microorganisms. Classification Classification can be defined as the arrangement of organisms into taxonomic groups (taxa) on the basis of similarities or relationships. Biochemical, physiologic, genetic and morphologic properties are often necessary for an adequate description of a taxon.