抄録
Circular dichroism spectra of haemoglobin Bart's (γ4) in the region from 240 to 600 nm were different from those of human adult haemoglobin, but closely similar to those of the β-subunit of human adult haemoglobin. The amplitude of the positive circular dichroism maximum of deoxygenated haemoglobin Bart's in the Soret region was much less than that of human adult haemoglobin. The peak molar extinction coefficient of deoxygenated haemoglobin Bart's in the Soret region was found to be lower than that of deoxygenated human adult haemoglobin. These data indicate that haemoglobin Bart's, which is composed of four identical chains and lacks co-operativity, is structurally similar to haemoglobin H (β4).
| 元の言語 | 英語 |
|---|---|
| ページ（範囲） | 365-369 |
| ページ数 | 5 |
| ジャーナル | Journal of Molecular Biology |
| 巻 | 65 |
| 発行部数 | 2 |
| DOI | |
| 出版物ステータス | 出版済み - 3 28 1972 |
| 外部発表 | Yes |
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All Science Journal Classification (ASJC) codes
- Structural Biology
- Molecular Biology
これを引用
Circular dichroism and absorption spectra of haemoglobin Bart's. / Sasazuki, Takehiko; Isomoto, Akio; Nakajima, Hiroshi.
：: Journal of Molecular Biology, 巻 65, 番号 2, 28.03.1972, p. 365-369.研究成果: ジャーナルへの寄稿 › 記事
}
TY - JOUR
T1 - Circular dichroism and absorption spectra of haemoglobin Bart's
AU - Sasazuki, Takehiko
AU - Isomoto, Akio
AU - Nakajima, Hiroshi
PY - 1972/3/28
Y1 - 1972/3/28
N2 - Circular dichroism spectra of haemoglobin Bart's (γ4) in the region from 240 to 600 nm were different from those of human adult haemoglobin, but closely similar to those of the β-subunit of human adult haemoglobin. The amplitude of the positive circular dichroism maximum of deoxygenated haemoglobin Bart's in the Soret region was much less than that of human adult haemoglobin. The peak molar extinction coefficient of deoxygenated haemoglobin Bart's in the Soret region was found to be lower than that of deoxygenated human adult haemoglobin. These data indicate that haemoglobin Bart's, which is composed of four identical chains and lacks co-operativity, is structurally similar to haemoglobin H (β4).
AB - Circular dichroism spectra of haemoglobin Bart's (γ4) in the region from 240 to 600 nm were different from those of human adult haemoglobin, but closely similar to those of the β-subunit of human adult haemoglobin. The amplitude of the positive circular dichroism maximum of deoxygenated haemoglobin Bart's in the Soret region was much less than that of human adult haemoglobin. The peak molar extinction coefficient of deoxygenated haemoglobin Bart's in the Soret region was found to be lower than that of deoxygenated human adult haemoglobin. These data indicate that haemoglobin Bart's, which is composed of four identical chains and lacks co-operativity, is structurally similar to haemoglobin H (β4).
UR - http://www.scopus.com/inward/record.url?scp=0015526787&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0015526787&partnerID=8YFLogxK
U2 - 10.1016/0022-2836(72)90287-2
DO - 10.1016/0022-2836(72)90287-2
M3 - Article
C2 - 5040362
AN - SCOPUS:0015526787
VL - 65
SP - 365
EP - 369
JO - Journal of Molecular Biology
JF - Journal of Molecular Biology
SN - 0022-2836
IS - 2
ER -