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  • Title: Purification of leghemoglobin from nodules of Crotalaria infected with Rhizobium.
    Author: Mendonça EH, Mazzafera P, Schiavinato MA.
    Journal: Phytochemistry; 1999 Jan; 50(2):313-6. PubMed ID: 9933947.
    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.
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