On the analogy in the structure of the spleen green heme protein and granulocyte myeloperoxidase

FEBS Letters

Ikeda-Saito, Masao¹ 

[1] Department of Biochemistry and Biophysics, University of Pennsylvania School of Medicine, Philadelphia, PA 19104-6089, USA

关键词: Myeloperoxidase;    Heme protein;    (Bovine spleen);   

DOI  :  10.1016/0014-5793(86)80695-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The molecular structure of the spleen green heme protein was reinvestigated by gel-permeation, SDS-polyacrylamide gel electrophoresis, and amino acid analysis. The results showed that the enzyme is a tetramer (M _r 1.5 × 10⁵) with two heavy subunits (M _r 6 × 10⁴ with a single prosthetic group per subunit) and two light subunits (M _r 1.5 × 10⁴), and that the tetramer structure is maintained by disulfide bond(s). The amino acid composition of the spleen green heme protein is similar to that of granulocyte myeloperoxidase. The present results contradict the data of Davis and Averill [(1981) J. Biol. Chem. 256, 5992-5996], who reported the enzyme as a monomeric peroxidase with an M _r of 57 000.

【 授权许可】

Unknown