A Method of Quantitation of Lactic Dehydrogenase in Agar Gel Electrophoresis

1965 ◽  
Vol 44 (2_ts) ◽  
pp. 231-233 ◽  
Author(s):  
John D. Mull ◽  
William H. Starkweather
1966 ◽  
Vol 21 (4) ◽  
pp. 352-356
Author(s):  
Yasuhiko Takamori ◽  
Yasuharu Hori ◽  
Kazuo Nishio

The enzyme activity and the electrophoretic characteristics of lactic dehydrogenase (LDH) in the plasma and different tissues from the mice with radiation-induced lymphoid leukaemia were examined and compared with those obtained from the normal mice. The LDH activity was abnormally increased in the leukaemic plasma. A considerable elevation of the enzyme level was also found both in the leukaemic spleen and in the lymphocytes isolated from it, but not in the liver, kidney, heart and muscle. LDH isozyme patterns were obtained by agar-gel electrophoresis. Each tissue exhibited a characteristic distribution of LDH activity among the separated isozymes. Leukaemic plasma contained much more LDH-5 than normal plasma, showing the pattern similar to that obtained from leukaemic spleen. Kidney and heart from leukaemic mice indicated no difference in the LDH-patterns as compared with those from normal mice.


The Lancet ◽  
1974 ◽  
Vol 304 (7892) ◽  
pp. 1321-1322
Author(s):  
W.H. Taylor ◽  
D.J. Etherington

Blood ◽  
1965 ◽  
Vol 25 (5) ◽  
pp. 830-838 ◽  
Author(s):  
VIRGINIA MINNICH ◽  
ROBERT J. HILL ◽  
PHILIP D. KHURI ◽  
MARY E. ANDERSON

Abstract A new hemoglobin, hemoglobin Hope, with a beta chain abnormality has been found in three generations of a St. Louis Negro family. The abnormal hemoglobin in the heterozygous state caused neither clinical stigmata nor abnormality in the red blood cells. Hemoglobin Hope was detected by agar gel electrophoresis at pH 6.2, but could not be differentiated from hemoglobin A by starch block electrophoresis at pH 8.6. Also, it could not be separated from hemoglobin A by paper, or starch gel electrophoresis employing a range of buffers from pH 6.2 to 8.6. Amino acid analysis showed that aspartic acid was substituted for glycine at position 136 of the beta chain. Hemoglobin Hope may be formulated as α2Aβ2136 gly-asp.


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