Please use this identifier to cite or link to this item:
Type: Artigo de periódico
Title: Purification of leghemoglobin from nodules of Crotalaria infected with Rhizobium
Author: Mendonca, EHM
Mazzafera, P
Schiavinato, MA
Abstract: The leghemoglobin from nodules of Crotalaria juncea infected with Rhizobium spp. was purified to homogeneity. The protein was purified after precipitation with 40-80% (NH4)(2)SO4, and chromatography by anionic exchange and gel filtration. The leghemoglobin has a single component and showed an apparent M-r of ca. 17,300 and 23,700 determined by SDS-PAGE and gel filtration, respectively. The amino acid composition showed that asparagine/aspartic acid, glutamine/glutamic acid, alanine, lysine, serine and leucine were the main amino acids. Iron was detected only in the band corresponding to the purified protein. The N-terminal amino acid sequence for the first 19 residues showed high similarities with several other leghemoglobins from other plants. (C) 1998 Elsevier Science Ltd. All rights reserved.
Subject: Crotalaria juncea
Country: Inglaterra
Editor: Pergamon-elsevier Science Ltd
Citation: Phytochemistry. Pergamon-elsevier Science Ltd, v. 50, n. 2, n. 313, n. 316, 1999.
Rights: fechado
Identifier DOI: 10.1016/S0031-9422(98)00532-9
Date Issue: 1999
Appears in Collections:Unicamp - Artigos e Outros Documentos

Files in This Item:
File Description SizeFormat 
WOS000078216500022.pdf201.72 kBAdobe PDFView/Open

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.