A comparison of the peroxidase isozymes of wheat plants grown at 6 °C and 20 °C

1969 ◽  
Vol 47 (2) ◽  
pp. 263-265 ◽  
Author(s):  
D. W. A. Roberts

The peroxidase isozymes from the first leaf of seven varieties of wheat of different levels of cold hardiness have been studied by agar gel electrophoresis. The plants were grown under controlled conditions at 6 °C or 20 °C. The isozyme pattern changes during ontogeny. The intensity of staining of the fastest moving "anionic" band is much greater in the leaves of the common wheats grown at 6 °C than in similar leaves from plants grown at 20 °C. This increase in peroxidase is apparently not associated with cold hardiness.

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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