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

Masao Ikeda-Saito

Research output: Contribution to journalArticlepeer-review

7 Citations (Scopus)

Abstract

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 (Mr 1.5 × 105) with two heavy subunits (Mr 6 × 104 with a single prosthetic group per subunit) and two light subunits (Mr 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 Mr of 57 000.

Original languageEnglish
Pages (from-to)245-250
Number of pages6
JournalFEBS Letters
Volume202
Issue number2
DOIs
Publication statusPublished - 1986 Jul 7

Keywords

  • (Bovine spleen)
  • Heme protein
  • Myeloperoxidase

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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