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Special problems encountered during the cyanogen bromide cleavage of lobster arginine kinase
Authors:C Richard  A Demarly  K K Han  M Dautrevaux
Affiliation:1. Laboratoire de Biochimie Structurale, Faculté de Médecine, Place de Verdun, 59045 Lille Cedex, France;2. Laboratoire de Chimie Générale, Faculté de Pharmacie, Rue du Professeur Laguesse, 59045 LilleCedex, France;1. Center for Human-Environment System Sustainability (CHESS), State Key Laboratory of Earth Surface Processes and Resource Ecology (ESPRE), Beijing Normal University, Beijing, 100875, China;2. School of Natural Resources, Faculty of Geographical Science, Beijing Normal University, Beijing, 100875, China;3. School of Life Sciences and School of Sustainability, Arizona State University, Tempe, AZ, 85287, USA;1. Jožef Stefan Institute, Department for Nanostructured Materials, Ljubljana, Slovenia;2. Vacuumschmelze GmbH & Co. KG, Hanau, Germany;1. School of Electric and Automation Engineering, Nanjing Normal University, No. 78 Bancang Street, Nanjing 210042, China;2. State Key Laboratory of Mechanics and Control of Mechanical Structures, Nanjing University of Aeronautics and Astronautics, No. 29 Yudao Street, Nanjing 210016, China;3. Institute of Fluid Science, Tohoku University, Katahira 2-1-1, Aoba-ku, Sendai, Miyagi 980-8577, Japan;1. College of Chemistry, Chemical Engineering and Materials Science, Soochow University, Suzhou 215123, PR China;2. College of Biological, Chemical Sciences and Engineering, Jiaxing University, Jiaxing, Zhejiang 314001, PR China
Abstract:During structural analysis of Lobster muscle arginine-kinase, we have isolated a CNBr resulting peptide with a blocked N-terminal residue. This peptide was sequenced after unblocking by mild acid treatment (1 N HCl at 100 degrees C for 10 min). The blocked form is not due to the formation of pyroglutamic acid nor is it due to the formation of diketopiperazine. We have applied the experimental conditions used for CNBr cleavage of lobster arginine-kinase to a synthetic peptide the structure of which is similar to the above CNBr peptide. We bring evidence that during CNBr cleavage partial formylation occurs with a possible cyclization of a 7 membered ring of Gly--Asp...
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