Eastern Kentucky University

Poster Title

Purification Of Rete Muscle From Mako Shark, Isurus oxyrinchus

Institution

Eastern Kentucky University

Abstract

Enolase is a glycolytic enzyme that is coded for by three genes, and thus exists in three forms αα, ββ, and γγ. Each form is active in the heart muscle and brain respectively. However it must be said that only the mentioned forms are in the said tissue, the genes that code for γγ are inactive in muscle and vice versa. The Mako shark, Isurus oxyrinchus, is a member of the makeral shark family and thus has a specialized muscle group called rete muscle. This red colored muscle contains the rete merabilae, an intertwining mass of arterioles and venules that create a counter current exchange system to help heat the sharks’ blood. Enolase was purified from this muscle after a purification of regular white mako shark muscle yielded a high enolase concentration. 11.44 mg of enolase were obtained showing .409 ABS specific activity. Two peaks of activity were found via DEAE ion exchange and isoelectric focus sing, suggesting protease activity within the muscle.

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Purification Of Rete Muscle From Mako Shark, Isurus oxyrinchus

Enolase is a glycolytic enzyme that is coded for by three genes, and thus exists in three forms αα, ββ, and γγ. Each form is active in the heart muscle and brain respectively. However it must be said that only the mentioned forms are in the said tissue, the genes that code for γγ are inactive in muscle and vice versa. The Mako shark, Isurus oxyrinchus, is a member of the makeral shark family and thus has a specialized muscle group called rete muscle. This red colored muscle contains the rete merabilae, an intertwining mass of arterioles and venules that create a counter current exchange system to help heat the sharks’ blood. Enolase was purified from this muscle after a purification of regular white mako shark muscle yielded a high enolase concentration. 11.44 mg of enolase were obtained showing .409 ABS specific activity. Two peaks of activity were found via DEAE ion exchange and isoelectric focus sing, suggesting protease activity within the muscle.