Isolation and characterization of a bacteriocin produced by Cicer-Rhizobium
A constitutively expressed bacteriocin from Cicer-Rhizobium was purified to homogeneity. The purified preparation yielded a homogenous protein with a molecular weight of about 29 kDa. This protein was heat stable, unaffected by nucleases and was found to have an iso-electric point (pI) of 4.6. The N...
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Veröffentlicht in: | World journal of microbiology & biotechnology 2001-11, Vol.17 (8), p.795-799 |
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