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|Type:||Artigo de periódico|
|Title:||Purification of leghemoglobin from nodules of Crotalaria infected with Rhizobium|
|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.|
|Editor:||Pergamon-elsevier Science Ltd|
|Citation:||Phytochemistry. Pergamon-elsevier Science Ltd, v. 50, n. 2, n. 313, n. 316, 1999.|
|Appears in Collections:||Unicamp - Artigos e Outros Documentos|
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