A New Unstable, High Oxygen Affinity Hemoglobin: Hb Nagoya Orβ97 (Fg4) His→Pro
作者:
OhbaY.,
ImanakaH.,
MatsuokaM.,
HattoriY.,
MiyajiT.,
FunakiC.,
ShibataK.,
ShimokataH.,
KuzuyaF.,
MiwaS.,
期刊:
Hemoglobin
(Taylor Available online 1985)
卷期:
Volume 9,
issue 1
页码: 11-24
ISSN:0363-0269
年代: 1985
DOI:10.3109/03630268508996978
出版商: Taylor&Francis
数据来源: Taylor
摘要:
An unstable hemoglobin was detected by isopropanol and heat precipitation tests in a 49-year-old Japanese man suffering from acute exacerbation of a chronic hemolytic disorder which was apparently triggered by infection of cholelithiasis. One of his two sons carried the same abnormal hemoglobin, and was jaundiced, but otherwise healthy, without anemia. The abnormal hemoglobin focused at a slightly more anodic position than Hb A in thin layer polyacrylamide gel electrofocusing. The abnormalβchain emerged after normalβchain in reverse phase high performance liquid chromatography of the hemolysate. It comprised 16.7 % and 25.5 % of the totalβchain in the propositus and his son, respectively.The partially heme-depleted abnormalβsubunit was precipitated with p-chloromercuribenzoic acid, and the abnormalβchain was isolated by urea CM-cellulose column chromatography. Structural analysis demonstrated substitution of proline for histidine at position 97 (FG4) in the e chain.The abnormal hemoglobin was purified by ion-exchange column chromatography. It showed a hyperbolic oxygen equilibrium curve indicating a high oxygen affinity and the absence of cooperative intersubunit interaction. Subunit dissociation seemed to be slightly enhanced. The variant was markedly susceptible to oxidation and rapidly lost heme upon oxidation.
点击下载:
PDF (560KB)
返 回