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.
You do not have subscription access to this journal. Cited by links are available to subscribers only. You may subscribe either as an OSA member, or as an authorized user of your institution.
Contact your librarian or system administrator
Login to access OSA Member Subscription