Characterization of terrain surface and mechanisms of shallow landsliding in upper Kurokawa watershed, Mt Aso, western Japan

2007 ◽  
Vol 67 (1) ◽  
pp. 87-95 ◽  
Author(s):  
Prem P. Paudel ◽  
H. Omura ◽  
T. Kubota ◽  
B. Devkota
Keyword(s):  
Western Japan ◽  
Terrain Surface

Detection and molecular characterization of Babesia sp. in wild boar (Sus scrofa) from western Japan

2021 ◽  
pp. 101695
Author(s):  
Momoko Morikawa ◽  
Sumire Mitarai ◽  
Isshu Kojima ◽  
Misuzu Okajima ◽  
Hitoshi Hatai ◽  
...  
Keyword(s):  
Wild Boar ◽  
Molecular Characterization ◽  
Sus Scrofa ◽  
Western Japan

scholarly journals Hemoglobin Hirose: α2β237(C3) Tryptophan Yielding Serine

Blood ◽  
1971 ◽  
Vol 38 (6) ◽  
pp. 730-738 ◽  
Author(s):  
KOTARO YAMAOKA
Keyword(s):  
Family Members ◽  
Chemical Characterization ◽  
The Third ◽  
The Family ◽  
Western Japan ◽  
Slow Moving ◽  
Clinically Significant ◽  
Β Chain ◽  
Screening Survey

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.

scholarly journals The Characterization of Hemoglobin Shimonoseki

Blood ◽  
1964 ◽  
Vol 24 (5) ◽  
pp. 624-635 ◽  
Author(s):  
M. HANADA ◽  
D. L. RUCKNAGEL
Keyword(s):  
Western Japan ◽  
A Minor ◽  
Polypeptide Chains

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.

scholarly journals CHARACTERIZATION OF A FAST MOVING ABNORMAL HEMOGLOBIN FROM WESTERN JAPAN (HB KAGOSHIMA)

1964 ◽  
Vol 53 (2) ◽  
pp. 188-194
Author(s):  
Yoshiro OHTA ◽  
Masashi SEITA ◽  
Ippei OHYA ◽  
Takashi IMAMURA ◽  
Motosuke HANADA
Keyword(s):  
Fast Moving ◽  
Western Japan ◽  
Abnormal Hemoglobin

Morphological Characterization of Mycobacteriophage R1

1974 ◽  
Vol 32 ◽  
pp. 254-255
Author(s):  
B. L. Soloff ◽  
T. A. Rado
Keyword(s):  
Carbon Source ◽  
Stationary Phase ◽  
Growth Phase ◽  
Minimal Medium ◽  
Morphological Characterization ◽  
Logarithmic Growth Phase ◽  
Complete Lysis ◽  
Lysogenic Culture ◽  
Logarithmic Growth

Mycobacteriophage R1 was originally isolated from a lysogenic culture of M. butyricum. The virus was propagated on a leucine-requiring derivative of M. smegmatis, 607 leu−, isolated by nitrosoguanidine mutagenesis of typestrain ATCC 607. Growth was accomplished in a minimal medium containing glycerol and glucose as carbon source and enriched by the addition of 80 μg/ ml L-leucine. Bacteria in early logarithmic growth phase were infected with virus at a multiplicity of 5, and incubated with aeration for 8 hours. The partially lysed suspension was diluted 1:10 in growth medium and incubated for a further 8 hours. This permitted stationary phase cells to re-enter logarithmic growth and resulted in complete lysis of the culture.

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