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- Alan N. Schechter
- National Inistitiutes of Health, Bethesda, Maryland 20014
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- Raymond F. Chen
- National Inistitiutes of Health, Bethesda, Maryland 20014
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- Christian B. Anfinsen
- National Inistitiutes of Health, Bethesda, Maryland 20014
抄録
<jats:p> Staphylococcal nuclease undergoes a reversible structural transition between <jats:italic>p</jats:italic> H3 and 4 which can be measured by changes in tryptophan fluorescence. A stopped-flow spectrofluorometer was used to study the kinetics of renaturation of nuclease from the acidified form on neutralization. The refolding is fast, and the data can be described as a sequence of two first-order processes, with half times of about 55 and 350 milliseconds, respectively. </jats:p>
収録刊行物
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- Science
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Science 167 (3919), 886-887, 1970-02-06
American Association for the Advancement of Science (AAAS)
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キーワード
詳細情報
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- CRID
- 1360574094907271168
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- NII論文ID
- 30020497085
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- ISSN
- 10959203
- 00368075
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- データソース種別
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