May 25, 1976

Antifreeze glycoproteins from Antarctic fish. Inactivation by borate

The Journal of Biological Chemistry
A I AhmedR E Feeney

Abstract

Antifreeze glycoprotein, which has previously been shown to be inactive in the presence of borate, migrates electrophoretically as the borate complex, presumably through formation of borate complexes with hydroxyl groups on the sugar side chains. Antifreeze glycoprotein (5 mg/ml) has been found to be completely active in the presence of 0.1 M borate at pH 7, but inactive at pH 9. A titration curve of pH versus the antifreeze activity of glycoprotein (5 mg/ml) in 0.1 M borate showed a progressive decrease in antifreeze activity as the pH was increased. Concomitant with decreases in activity were increases in binding of borate. At pH 9.0, nearly 2 mol of borate were complexed per glycotripeptide. Ultracentrifuge analyses showed similar molecular weights and laser quasi-elastic light scattering showed similar diffusions at pH 7.0 and 9.0 in borate and in the absence of borate. The binding of borate, rather than a change in conformation, is thus directly related to the loss of antifreeze activity. Alkaline borate also decreased hemagglutinating activity of Osage orange lectin and decreased the inhibition of the activity by the antifreeze glycoproteins.

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Mentioned in this Paper

Hemagglutination
Plasma Protein Binding Capacity
Neoglycoproteins
Aldehydes
Polymers
Protein Conformation
Borates
Animal Lectins
Melting
Hydrogen-Ion Concentration

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