Methemoglobin Reductase in Human Erythrocyte

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概要

• 論文の詳細を見る

• NADH-Methemoglobin reductase was purified 40,000-fold from human erythrocytes in the form of a simple protein without a prosthetic group or a metal, having the molecular weight of about 30,000. The enzyme showed NADH-diaphorase activity, and reduced metmyoglobin and ferric cytochrome c as quickly as methemoglobin. The rate of reduction of cytochrome b<SUB>5</SUB> by the enzyme is higher than that of methemoglobin, and the methemoglobin reduction is augumented in the presence of a catalytic amount of cytochrome b<SUB>5</SUB>. In view of Kms for NADH and methemoglobin, the enzyme seems to play a major role in the reduction of methemoglobin in erythrocytes.

• Japan Society of Clinical Chemistryの論文

著者

• 杉田 良樹

  金沢大学医学部生化学

• 米山 良昌

  金沢大学医学部生化学

• 野村 誠一

  金沢大学医学部第一生化学

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• Methemoglobin Reductase in Human Erythrocyte

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