A Substitute for Ortho-Tolidine in the Detection of Haptoglobin Phenotypes

Burdett, P.E.

doi:10.1016/s0015-7368(77)71112-0

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Materials and Methods Enzyme Preparation1

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1983

1988

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“…Only the major band was stained by Leucomalachite Green (Burdett, 1977). The preparation was therefore judged to be free of other haemoproteins.…”

Section: Materials and Methods Enzyme Preparationmentioning

confidence: 99%

Lactoperoxidase haem, an iron-porphyrin thiol

Nichol¹,

Angel²,

Moon³

et al. 1987

Biochemical Journal

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The haem prosthetic group of lactoperoxidase can be prepared from the enzyme in high yield by reductive cleavage with mercaptoethanol in 8 M-urea under mild conditions. The product yields porphyrins, after removal of iron, which show visible spectroscopic properties similar to protoporphyrin but are considerably more polar. In the presence of iodoacetamide, a different product is obtained by reductive cleavage. The proton n.m.r. and mass spectra of this compound indicate that the prosthetic group of the enzyme is the iron complex of 18-mercaptomethyl-2,7,12-trimethyl-3,8-divinylporphyrin-13,17-d ipropionic acid. It is proposed that the unusual strength of binding of the prosthetic group to the apoprotein is due to formation of a disulphide bond from a cysteine residue to the porphyrin thiol.

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“…Only the major band was stained by Leucomalachite Green (Burdett, 1977). The preparation was therefore judged to be free of other haemoproteins.…”

Section: Materials and Methods Enzyme Preparationmentioning

confidence: 99%