Literature DB >> 2538448

Demonstration that spleen green hemeprotein is identical to granulocyte myeloperoxidase.

M Ikeda-Saito1, H C Lee, K Adachi, H S Eck, R C Prince, K S Booth, W S Caughey, S Kimura.   

Abstract

The biochemical, spectroscopic, enzymatic, and redox properties of spleen myeloperoxidase, a peroxidase formerly called "spleen green hemeprotein," and granulocyte myeloperoxidase were compared by electrophoresis, amino-terminal amino acid sequences, optical and EPR spectroscopy, steady-state enzyme kinetics, and oxidation-reduction potential. The spleen enzyme exhibits properties indistinguishable from those of the granulocyte enzyme. We conclude that the spleen enzyme is indeed identical to granulocyte myeloperoxidase.

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Year:  1989        PMID: 2538448

Source DB:  PubMed          Journal:  J Biol Chem        ISSN: 0021-9258            Impact factor:   5.157


  2 in total

1.  Evidence that a formyl-substituted iron porphyrin is the prosthetic group of myeloperoxidase: magnetic circular dichroism similarity of the peroxidase to Spirographis heme-reconstituted myoglobin.

Authors:  M Sono; A M Bracete; A M Huff; M Ikeda-Saito; J H Dawson
Journal:  Proc Natl Acad Sci U S A       Date:  1991-12-15       Impact factor: 11.205

2.  Characterization of bovine neutrophil antibacterial polypeptides which bind to Escherichia coli.

Authors:  L Litteri; D Romeo
Journal:  Infect Immun       Date:  1993-03       Impact factor: 3.441

  2 in total

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