Purification Of Leghemoglobin From Nodules Of Crotalaria Infected With Rhizobium.

dc.creatorMendonça, E H
dc.creatorMazzafera, P
dc.creatorSchiavinato, M A
dc.date1999-Jan
dc.date2015-11-27T12:19:32Z
dc.date2015-11-27T12:19:32Z
dc.date.accessioned2018-03-29T00:53:23Z
dc.date.available2018-03-29T00:53:23Z
dc.identifierPhytochemistry. v. 50, n. 2, p. 313-6, 1999-Jan.
dc.identifier0031-9422
dc.identifier
dc.identifierhttp://www.ncbi.nlm.nih.gov/pubmed/9933947
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/194331
dc.identifier9933947
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1294564
dc.descriptionThe 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.
dc.description50
dc.description313-6
dc.languageeng
dc.relationPhytochemistry
dc.relationPhytochemistry
dc.rightsfechado
dc.rights
dc.sourcePubMed
dc.subjectAmino Acid Sequence
dc.subjectAmino Acids
dc.subjectChromatography, Gel
dc.subjectChromatography, Ion Exchange
dc.subjectElectrophoresis, Polyacrylamide Gel
dc.subjectFabaceae
dc.subjectLeghemoglobin
dc.subjectMolecular Sequence Data
dc.subjectMolecular Weight
dc.subjectPlants, Medicinal
dc.subjectRhizobium
dc.titlePurification Of Leghemoglobin From Nodules Of Crotalaria Infected With Rhizobium.
dc.typeArtículos de revistas


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