ミオグロビンに関する研究
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- 安井 勉
- 北海道大学農学部 畜産学科
書誌事項
- タイトル別名
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- Studies on Myoglobin
- IV Spectrophotometric Observations on Heat Denaturation of Myoglobin
- IV ミオグロビンの加熱変性の分光化学的観察
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説明
In order to investigate the state of cooked myoglobin which has beeen known as the main constituent of meat color in cooked cured meat, experiments on heat denaturation or coagulation of myoglobin were carried out by using cristallized metmyoglobin as a sample.<br>From these experiments, the following facts were found out.<br>(1) Myoglobin was hardly denatured in 1/10M NaOH in which hemoglobin was denatured.<br>(2) When beat-coagulated myoglobin was dissolved in 1/10M NaOH solution and then neutralized, a native myoglobin-like substance, which showed photometrically the characteristics identical with those of native myoglobin, was obtained. The yields were about 80% after 5 minutes, and 40-50% after 30 minutes, heating at 100° in distilled water, 60-70% after 5 minutes, and 40-50% after 30 minutes, heating at 100° in 1/10M phosphate buffer (pH 7.0), and about 20% after 5 minutes, and 10-18% after 30 minutes, heating at 100° in 3% NaCl solution<br>(3) Heat-coagulated nitric-oxide myoglobin dissolved in 1/10M NaOH solution showed a spectral curve similar to that of native myoglobin. Myoglobin derivatives dissolved in the same solution gave the same results.<br>(4) Myoglobin recovered from heat-coagulated metmyoglobin could form various derivatives as native myoglobin could and the spectral characteristics of each derivative showed good agreement with those of native myoglobin.<br>(5) From these results, it is supposed theat the heat-denaturation of myoglobin consists of two processes; that is, the reversible and the irreversible one.
収録刊行物
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- 日本畜産学会報
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日本畜産学会報 29 (3), 163-167, 1958
公益社団法人 日本畜産学会
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詳細情報 詳細情報について
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- CRID
- 1390282680169144064
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- NII論文ID
- 130000735413
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- ISSN
- 18808255
- 1346907X
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- 本文言語コード
- ja
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- データソース種別
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- JaLC
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- 使用不可