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

Comparative Biochemistry and Physiology Part B: Comparative Biochemistry Pub Date : 1994-12-01 DOI:10.1016/0305-0491(94)90126-0

P. Becuwe , J. van Beeumen , B. Samyn , J.P. Touzel , C. Slomianny , D. Camus , D. Dive

引用次数: 5

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.

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巴贝斯虫超氧化物歧化酶的纯化、鉴定及氨基末端序列分析

结果发现，巴贝斯虫含有两种超氧化物歧化酶(SOD)同工酶，等电点(pI)分别为4.9和5.2。这两个同工酶(45和47 kDa)由两个22 kDa的亚基组成。从这些同工酶的34个残基中确定了一个独特的氨基末端序列，并鉴定为SOD序列。该n端序列与已知的29个Fe-或mn -SOD进行比较，发现与Fe-SOD具有更多的同源性。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

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Comparative Biochemistry and Physiology Part B: Comparative Biochemistry

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