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Thyroxine deiodination associated with NADPH-dependent lipid peroxidation in a submicrosomal system

Proceedings of the Society for Experimental Biology and Medicine

Nov 1, 1975

K Suwa, Masahiko Nakano

PMID: 1791

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Abstract

A lipoprotein present in trypsin-treated microsomes can be oxidized with formation of malondialdehyde in a system which contains NADPH, ferric ion-ADP complex, NADPH-cytochrome c reductase and a factor. This factor, a mixture of peptides, can be isolated from hepatic microsomes by tryps...read more

Mentioned in this Paper

Thyroxine
Sephadex G 100
Lipoprotein (a)
NADP
Total Thyroxine Measurement
Thyroxine Measurement
Digestion
Trypsin
Deiodination
Iron

Thyroxine deiodination associated with NADPH-dependent lipid peroxidation in a submicrosomal system

Proceedings of the Society for Experimental Biology and Medicine

Nov 1, 1975

K Suwa, Masahiko Nakano

PMID: 1791

DOI:

Abstract

A lipoprotein present in trypsin-treated microsomes can be oxidized with formation of malondialdehyde in a system which contains NADPH, ferric ion-ADP complex, NADPH-cytochrome c reductase and a factor. This factor, a mixture of peptides, can be isolated from hepatic microsomes by tryps...read more

Mentioned in this Paper

Thyroxine
Sephadex G 100
Lipoprotein (a)
NADP
Total Thyroxine Measurement

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