Results 181 to 190 of about 18,599 (219)
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Hemocyanin of the chiton Acanthopleura granulata
Biochemistry, 1986The subunit structure and solution conformation of the hemocyanin of the chiton Acanthopleura granulata were investigated by light-scattering, ultracentrifugation, viscosity, absorbance, and circular dichroism methods. The molecular weight, determined by light scattering at pH 7.4 in the presence of 0.05 M Mg2+ and 0.01 M Ca2+, was (4.2 +/- 0.3) X 10(6)
T T, Herskovits +2 more
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Conversion of crustacean hemocyanin to catecholoxidase
Micron, 2004Crustacean hemocyanin as oxygen carrier and catecholoxidase as enzymes belong to the same protein family (type 3 copper proteins) sharing very similar active sites. Treatment with SDS of these hemocyanins results in an opening of the entrance to the active site for bulky phenolic compounds. This demonstrates, that almost all hemocyanin subunits possess
Elmar, Jaenicke, Heinz, Decker
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Hemocyanins of the Gastropods.
The Journal of Physical and Colloid Chemistry, 1947openaire +2 more sources
Circular Dichroism of Hemocyanin
The Journal of Biochemistry, 1968H, Takesada, K, Hamaguchi
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Immunogenicity of hemocyanin for the mouse
Immunochemistry, 1970S, Malkiel, B J, Hargis
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The binding of copper by hemocyanin
Journal of Cellular and Comparative Physiology, 1954openaire +2 more sources
Processing of crayfish hemocyanin subunits into phenoloxidase
Biochemical and Biophysical Research Communications, 2004Bok Luel Lee, Kenneth Söderhäll
exaly