PURIFICATION, CHARACTERIZATION AND AMINO-TERMINAL SEQUENCE OF THE SUPEROXIDE-DISMUTASE FROM BABESIA-HYLOMYSCI

被引：6

作者：

BECUWE, P

VANBEEUMEN, J

SAMYN, B

TOUZEL, JP

SLOMIANNY, C

CAMUS, D

DIVE, D

机构：

[1] DOMAINE CERTIA, INSERM, U42, F-59651 VILLENEUVE DASCQ, FRANCE

[2] STATE UNIV GHENT, DEPT BIOCHEM PHYSIOL & MICROBIOL, B-9000 GHENT, BELGIUM

[3] INRA, F-59651 VILLENEUVE DASCQ, FRANCE

来源：

COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY | 1994年 / 109卷 / 04期

关键词：

BABESIA HYLOMYSCI; PARASITE; RODENT; SUPEROXIDE DISMUTASE; IRON; N-TERMINAL SEQUENCE; OXIDANT STRESS;

D O I：

10.1016/0305-0491(94)90126-0

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：637 / 645

页数：9

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