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Purification, characterization and amino terminal sequence of the superoxide dismutase from Babesia hylomysci

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Abstract
Babesia hylomysci was found to contain two superoxide dismutase (SOD) isoenzymes with isoelectric points (pI) of 4.9 and 5.2. The two isoenzymes (45 and 47 kDa) were composed of two subunits of 22 kDa. An unique amino terminal sequence was determined up to 34 residues from the pooled isoenzymes and was identified as a sequence of SOD. The comparison of this N-terminal sequence of B. hylomysci SOD with 29 known Fe- or Mn-SODs showed more homologies with Fe-SODs.
Keywords
PARASITE, BABESIA HYLOMYSCI, RODENT, SUPEROXIDE DISMUTASE, IRON, N-TERMINAL SEQUENCE, OXIDANT STRESS, ANABAENA-CYLINDRICA LEMM, IRON-SUPEROXIDE, TRITRICHOMONAS-FOETUS, LOCALIZATION, HETEROCYSTS, EUCARYOTE, ENZYME

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MLA
Becuwe, P., et al. “Purification, Characterization and Amino Terminal Sequence of the Superoxide Dismutase from Babesia Hylomysci.” COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY, vol. 109, no. 4, 1994, pp. 637–45, doi:10.1016/0305-0491(94)90126-0.
APA
Becuwe, P., Van Beeumen, J., Samyn, B., Touzel, J., Slomianny, C., Camus, D., & Dive, D. (1994). Purification, characterization and amino terminal sequence of the superoxide dismutase from Babesia hylomysci. COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY, 109(4), 637–645. https://doi.org/10.1016/0305-0491(94)90126-0
Chicago author-date
Becuwe, P, Jozef Van Beeumen, Bart Samyn, JP Touzel, C Slomianny, D Camus, and D Dive. 1994. “Purification, Characterization and Amino Terminal Sequence of the Superoxide Dismutase from Babesia Hylomysci.” COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY 109 (4): 637–45. https://doi.org/10.1016/0305-0491(94)90126-0.
Chicago author-date (all authors)
Becuwe, P, Jozef Van Beeumen, Bart Samyn, JP Touzel, C Slomianny, D Camus, and D Dive. 1994. “Purification, Characterization and Amino Terminal Sequence of the Superoxide Dismutase from Babesia Hylomysci.” COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY 109 (4): 637–645. doi:10.1016/0305-0491(94)90126-0.
Vancouver
1.
Becuwe P, Van Beeumen J, Samyn B, Touzel J, Slomianny C, Camus D, et al. Purification, characterization and amino terminal sequence of the superoxide dismutase from Babesia hylomysci. COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY. 1994;109(4):637–45.
IEEE
[1]
P. Becuwe et al., “Purification, characterization and amino terminal sequence of the superoxide dismutase from Babesia hylomysci,” COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY, vol. 109, no. 4, pp. 637–645, 1994.
@article{191872,
  abstract     = {{Babesia hylomysci was found to contain two superoxide dismutase (SOD) isoenzymes with isoelectric points (pI) of 4.9 and 5.2. The two isoenzymes (45 and 47 kDa) were composed of two subunits of 22 kDa. An unique amino terminal sequence was determined up to 34 residues from the pooled isoenzymes and was identified as a sequence of SOD. The comparison of this N-terminal sequence of B. hylomysci SOD with 29 known Fe- or Mn-SODs showed more homologies with Fe-SODs.}},
  author       = {{Becuwe, P and Van Beeumen, Jozef and Samyn, Bart and Touzel, JP and Slomianny, C and Camus, D and Dive, D}},
  issn         = {{0305-0491}},
  journal      = {{COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY}},
  keywords     = {{PARASITE,BABESIA HYLOMYSCI,RODENT,SUPEROXIDE DISMUTASE,IRON,N-TERMINAL SEQUENCE,OXIDANT STRESS,ANABAENA-CYLINDRICA LEMM,IRON-SUPEROXIDE,TRITRICHOMONAS-FOETUS,LOCALIZATION,HETEROCYSTS,EUCARYOTE,ENZYME}},
  language     = {{eng}},
  number       = {{4}},
  pages        = {{637--645}},
  title        = {{Purification, characterization and amino terminal sequence of the superoxide dismutase from Babesia hylomysci}},
  url          = {{http://doi.org/10.1016/0305-0491(94)90126-0}},
  volume       = {{109}},
  year         = {{1994}},
}

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