Characterization of 210Pb and 137Cs radionuclides in sediment from Lake Shinji, Shimane Prefecture, western Japan

2011 ◽  
Vol 69 (2) ◽  
pp. 455-462 ◽  
Author(s):  
Yutaka Kanai
2021 ◽  
pp. 101695
Author(s):  
Momoko Morikawa ◽  
Sumire Mitarai ◽  
Isshu Kojima ◽  
Misuzu Okajima ◽  
Hitoshi Hatai ◽  
...  

Blood ◽  
1971 ◽  
Vol 38 (6) ◽  
pp. 730-738 ◽  
Author(s):  
KOTARO YAMAOKA

Abstract During an electrophoretic screening survey for hemoglobinopathies in western Japan, a slow-moving variant of hemoglobin A, to be designated hemoglobin Hirose, was found in a family of Japanese origin. Chemical characterization of hemoglobin Hirose revealed that tryptophan at the 37th position of the β-chain was replaced by serine, the third residue of C-helix of the β-chain involving contacts between αl and β2 subunits. Even though the oxygen equilibrium of this hemoglobin was abnormal, none of the family members showed any clinically significant symptoms.


Blood ◽  
1964 ◽  
Vol 24 (5) ◽  
pp. 624-635 ◽  
Author(s):  
M. HANADA ◽  
D. L. RUCKNAGEL

Abstract Hemoglobin Shimonoseki, discovered in western Japan in 1960, has been further characterized as a mutant with abnormal α-polypeptide chains on the basis of: (1) The presence of a minor hemoglobin component migrating cathodally at pH 8.6 to Hb A2, presumably α2Shσ2A2. (2) Hybridization studies. (3) Fingerprinting of isolated α-polypeptide chains. Hemoglobin Sh is characterized by the substitution of arginine for glutamine at residue 54 and can therefore be designated as α254Argβ2A.


1964 ◽  
Vol 53 (2) ◽  
pp. 188-194
Author(s):  
Yoshiro OHTA ◽  
Masashi SEITA ◽  
Ippei OHYA ◽  
Takashi IMAMURA ◽  
Motosuke HANADA

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