PRIMARY STRUCTURE OF BOVINE LACTOPEROXIDASE, A 4TH MEMBER OF A MAMMALIAN HEME PEROXIDASE FAMILY

被引:106
作者
CALS, MM [1 ]
MAILLIART, P [1 ]
BRIGNON, G [1 ]
ANGLADE, P [1 ]
DUMAS, BR [1 ]
机构
[1] INRA,PROT UNIT,BAT 224,F-78352 JOUY EN JOSAS,FRANCE
来源
EUROPEAN JOURNAL OF BIOCHEMISTRY | 1991年 / 198卷 / 03期
关键词
D O I
10.1111/j.1432-1033.1991.tb16073.x
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
Much is known about bovine lactoperoxidase but no data are available on its primary structure. In this work its main active fraction was isolated from cow's milk and sequenced using a conventional strategy. A clear similarity was found with human myeloperoxidase, eosinophil peroxidase and thyroperoxidase, the sequences of which were recently elucidated from those of their cDNAs and/or genes. The single peptide chain of bovine lactoperoxidase contains 612 amino acid residues, including 15 half-cystines and 4 or 5 potential N-glycosylation sites. The corresponding peptide segments of human myeloperoxidase, eosinophil peroxidase and thyroperoxidase display 55%, 54% and 45% identity with bovine lactoperoxidase, respectively, with 14 out of the 15 half-cystines present in each of the four enzymes being located in identical positions. The occurrence of an odd number of half-cystines in bovine lactoperoxidase supports the recent finding of a heme thiol released from this enzyme by a reducing agent, suggesting that the heme is bound to the peptide chain via a disulfide linkage, since the absence of free thiol in the enzyme was reported long ago.
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收藏
页码:733 / 739
页数:7
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