Sunday 8 July 2012

CyprinidaeBarbus

CyprinidaeBarbus

Hemoglobin is a tetrameric protein with two alpha and two beta subunits binds oxygen in a cooperative manner. In dominant tetrameric form of fish hemoglobin carry more than 90 percent of oxygen from gill to tissues at 20° C. The tetrameric form of fish hemoglobin is changed to monomeric form at low oxygen pressure in order to increase its oxygen affinity. This is one of adaptive mechanisms used by different kinds of fish. The major aim of this paper is to study the molecular basis of shirbot hemoglobin adaptation mechanism to various environmental conditions. Using different methods such as ion exchange chromatography, UV-Vis, fluorescence and circular dichroism spectroscopy, we extracted the main tetrameric fraction of shirbot hemoglobin and studied the structural characteristics of shirbot and human hemoglobins in a comparative way

Cyprinidae Barbus

Cyprinidae Barbus

Cyprinidae Barbus

Cyprinidae Barbus

Cyprinidae Barbus

Cyprinidae Barbus

Cyprinidae Barbus

Cyprinidae Barbus

Cyprinidae Barbus

Cyprinidae Barbus

Cyprinidae Barbus

Cyprinidae Barbus

Cyprinidae Barbus

Cyprinidae Barbus

Cyprinidae Barbus

Cyprinidae Barbus



Cyprinidae Barbus


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