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Human growth hormone denaturation

Zhao, E, E. Ghezzo-Schoneich, G.I. Aced, J. Hong, T. MUby, and C. Schoneich, Metal-catalyzed oxidation of histidine in human growth hormone. Mechanism, isotope effects, and inhibition by a mild denaturing alcohol. J Biol Chem, 1997.272(14) 9019-29. [Pg.62]

For liquid formulations, shaking the formulation increases the air/liquid interface in the formulation and often leads to protein denaturation. Several proteins are susceptible to denaturation by shaking, including human growth hormone (hGH) and recombinant factor XIII, both of which formed insoluble aggregates after shaking. [Pg.283]

See other pages where Human growth hormone denaturation is mentioned: [Pg.707]    [Pg.714]    [Pg.350]    [Pg.128]    [Pg.34]    [Pg.145]    [Pg.168]    [Pg.401]    [Pg.975]    [Pg.92]    [Pg.147]    [Pg.190]    [Pg.183]   
See also in sourсe #XX -- [ Pg.39 ]



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