抄録
The interactions of urea, trimethylamine-N-oxide (TMAO), and related solutes on a number of enzymes were examined. Urea inhibited enzymatic activity and accelerated the thermal inactivation of catalase, whereas TMAO activated some enzymes but inhibited others. The effects of urea and of TMAO, whether parallel or in opposition, were exerted independently. Thus, in those cases where TMAO increases enzymatic activity, it did so to the same relative degree, whether or not urea was present. TMAO markedly decreased the rate of thermal inactivation of catalase, indicating that it does favor compact protein structures. The assumption that TMAO factors compaction of protein structure, whereas urea has the contrary effect, does not lead to the expectation that TMAO must always oppose the effect of urea on enzymatic activity, since the most compact form of an enzyme may not always be the most active form.
| 元の言語 | English |
|---|---|
| ページ（範囲） | 356-360 |
| ページ数 | 5 |
| ジャーナル | Archives of Biochemistry and Biophysics |
| 巻 | 258 |
| 発行部数 | 2 |
| DOI | |
| 出版物ステータス | Published - 1987 11 1 |
| 外部発表 | Yes |
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ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Molecular Biology
これを引用
Effects of urea and trimethylamine-N-oxide on enzyme activity and stability. / Mashino, Tadahiko; Fridovich, Irwin.
：: Archives of Biochemistry and Biophysics, 巻 258, 番号 2, 01.11.1987, p. 356-360.研究成果: Article
}
TY - JOUR
T1 - Effects of urea and trimethylamine-N-oxide on enzyme activity and stability
AU - Mashino, Tadahiko
AU - Fridovich, Irwin
PY - 1987/11/1
Y1 - 1987/11/1
N2 - The interactions of urea, trimethylamine-N-oxide (TMAO), and related solutes on a number of enzymes were examined. Urea inhibited enzymatic activity and accelerated the thermal inactivation of catalase, whereas TMAO activated some enzymes but inhibited others. The effects of urea and of TMAO, whether parallel or in opposition, were exerted independently. Thus, in those cases where TMAO increases enzymatic activity, it did so to the same relative degree, whether or not urea was present. TMAO markedly decreased the rate of thermal inactivation of catalase, indicating that it does favor compact protein structures. The assumption that TMAO factors compaction of protein structure, whereas urea has the contrary effect, does not lead to the expectation that TMAO must always oppose the effect of urea on enzymatic activity, since the most compact form of an enzyme may not always be the most active form.
AB - The interactions of urea, trimethylamine-N-oxide (TMAO), and related solutes on a number of enzymes were examined. Urea inhibited enzymatic activity and accelerated the thermal inactivation of catalase, whereas TMAO activated some enzymes but inhibited others. The effects of urea and of TMAO, whether parallel or in opposition, were exerted independently. Thus, in those cases where TMAO increases enzymatic activity, it did so to the same relative degree, whether or not urea was present. TMAO markedly decreased the rate of thermal inactivation of catalase, indicating that it does favor compact protein structures. The assumption that TMAO factors compaction of protein structure, whereas urea has the contrary effect, does not lead to the expectation that TMAO must always oppose the effect of urea on enzymatic activity, since the most compact form of an enzyme may not always be the most active form.
UR - http://www.scopus.com/inward/record.url?scp=0023444286&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0023444286&partnerID=8YFLogxK
U2 - 10.1016/0003-9861(87)90355-9
DO - 10.1016/0003-9861(87)90355-9
M3 - Article
C2 - 3674879
AN - SCOPUS:0023444286
VL - 258
SP - 356
EP - 360
JO - Archives of Biochemistry and Biophysics
JF - Archives of Biochemistry and Biophysics
SN - 0003-9861
IS - 2
ER -