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

Masao Ikeda-Saito

doi:10.1016/0014-5793(86)80695-0

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

Masao Ikeda-Saito

Institute of Multidisciplinary Research for Advanced Materials (IMRAM)

Research output: Contribution to journal › Article › peer-review

8 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 (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.

Original language	English
Pages (from-to)	245-250
Number of pages	6
Journal	FEBS Letters
Volume	202
Issue number	2
DOIs	https://doi.org/10.1016/0014-5793(86)80695-0
Publication status	Published - 1986 Jul 7

Keywords

(Bovine spleen)
Heme protein
Myeloperoxidase

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

Access to Document

10.1016/0014-5793(86)80695-0

Cite this

@article{2901aed2078544f6866773d6841b0291,

title = "On the analogy in the structure of the spleen green heme protein and granulocyte myeloperoxidase",

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.",

keywords = "(Bovine spleen), Heme protein, Myeloperoxidase",

author = "Masao Ikeda-Saito",

year = "1986",

month = jul,

day = "7",

doi = "10.1016/0014-5793(86)80695-0",

language = "English",

volume = "202",

pages = "245--250",

journal = "FEBS Letters",

issn = "0014-5793",

publisher = "Elsevier",

number = "2",

}

TY - JOUR

T1 - On the analogy in the structure of the spleen green heme protein and granulocyte myeloperoxidase

AU - Ikeda-Saito, Masao

PY - 1986/7/7

Y1 - 1986/7/7

N2 - 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.

AB - 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.

KW - (Bovine spleen)

KW - Heme protein

KW - Myeloperoxidase

UR - http://www.scopus.com/inward/record.url?scp=0022513977&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0022513977&partnerID=8YFLogxK

U2 - 10.1016/0014-5793(86)80695-0

DO - 10.1016/0014-5793(86)80695-0

M3 - Article

C2 - 3013687

AN - SCOPUS:0022513977

SN - 0014-5793

VL - 202

SP - 245

EP - 250

JO - FEBS Letters

JF - FEBS Letters

IS - 2

ER -

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

Abstract

Keywords

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this