Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/194331
Type: Artigo de periódico
Title: Purification Of Leghemoglobin From Nodules Of Crotalaria Infected With Rhizobium.
Author: Mendonça, E H
Mazzafera, P
Schiavinato, M A
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)2SO4, 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.
Subject: Amino Acid Sequence
Amino Acids
Chromatography, Gel
Chromatography, Ion Exchange
Electrophoresis, Polyacrylamide Gel
Fabaceae
Leghemoglobin
Molecular Sequence Data
Molecular Weight
Plants, Medicinal
Rhizobium
Rights: fechado
Identifier DOI: 
Address: http://www.ncbi.nlm.nih.gov/pubmed/9933947
Date Issue: 1999
Appears in Collections:Artigos e Materiais de Revistas Científicas - Unicamp

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