Abstract

An infrared spectroscopic method was used to study the hydrogen–deuterium exchange of a glycoprotein, bovine submaxillary mucin (BSM), dissolved in D<sub>2</sub>O. The <i>p</i>H-dependence of the rate and extent of the H–D exchange of BSM was determined. The rate constant of the exchange decreased as <i>p</i>H increased from 3.7 to 5.3 and remained constant at a minimum value, (0.82±0.09) × 10<sup>−2</sup> min<sup>−1</sup>, from <i>p</i>H 5.3 to 7.2. The extent of the exchange decreased with increasing <i>p</i>H in the <i>p</i>H range 3.7 to 5.3 and levelled off from <i>p</i>H 5.3 to 7.2. It is suggested that these results are due to a <i>p</i>H-dependent conformational change.

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