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ID 17377
Eprint ID
17377
FullText URL
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Title Alternative
Homogeneity of erythrocyte catalase and its stability to SDS and to LIS in acatalasemia and hypocatalasemia mice
Author
Mizugaki, Junko
Abstract
Behavior of hemoglobin in the erythrocytes to the addition of H(2)O(2) in saline was examined to be confirmed the equal distribution of catalase in erythrocyte population from acatalasemic heterozygote mouse (Cs(a)Cs(b)) which showed the half of normal (Cs(a)Cs(a)) catalase activity. When H(2)O(2) was added in the suspension mixed erythrocytes with Cs(a)Cs(a) and acatalasemia (Cs(b)Cs(b)), the color changed immediately from red to brownish red with emitting a little buble of O(2). One population of erythrocyte lacking catalase activity should be caused the methemoglobin formation. In fact, rapid spectrophotometric scanning proved that the wave length of maximum absorbance were 500nm and 630nm. When H(2)O(2) was added in the erythrocyte suspension from Cs(a)Cs(b), the color unchanged, remained red, with emitting bubles of O(2). This result was the same as in the erythrocyte suspension from Cs(a)Cs(a). Data indicated that erythrocyte from heterozygote (Cs(a)Cs(b)) is consist of one population and is not two populations of Cs(a)Cs(a) and Cs(b)Cs(b). The nature of blood catalase by stability to the surfactant (SDS and LIS) was compared among normal (Cs(a)Cs(a)), acatalasemic homozygote and heterozygote (Cs(b)Cs(b) and Cs(a)Cs(b)), and hypocatalasemic homozygote and heterozygote (Cs(c)Cs(c) and Cs(a)Cs(c)) mice. In both respects of SDS and LIS stability, Cs(a)Cs(a) was most stable and two heterozygotes (Cs(a)Cs(b) and Cs(a)Cs(c)) were less stable than Cs(a)Cs(a). Cs(c)Cs(c) and Cs(b)Cs(b), namely Cs(b)Cs(b) were of least stability to SDS and to LIS. It was demonstrated that blood catalase molecule of acatalasemic and hypocatalasemic heterozygote (Cs(a)Cs(b) and Cs(a)Cs(c)) differs from that of both parents (Cs(a)(Cs(a), Cs(b)Cs(b) and Cs(a)Cs(c)). It was concluded that 5 sorts of blood catalase were different each other and consist of a single molecular species and suggested that since catalase was a tetramer, the combination of subunits was different each other.
Published Date
1978-08
Publication Title
岡山医学会雑誌
Publication Title Alternative
Journal of Okayama Medical Association
Volume
volume90
Issue
issue7-8
Publisher
岡山医学会
Publisher Alternative
Okayama Medical Association
Start Page
785
End Page
793
ISSN
0030-1558
NCID
AN00032489
Content Type
Journal Article
Official Url
https://www.jstage.jst.go.jp/article/joma1947/90/7-8/90_7-8_785/_article/-char/ja/
Related Url
http://www.okayama-u.ac.jp/user/oma/
language
日本語
Copyright Holders
岡山医学会
File Version
publisher
Refereed
True
Eprints Journal Name
joma