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Biophysical Journal 63: 1240-1243 (1992)
© 1992 the Biophysical Society

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Matrix-assisted laser desorption mass spectrometry of rhodopsin and bacteriorhodopsin.

K L Schey, D I Papac, D R Knapp and R K Crouch

Department of Pharmacology, Medical University of South Carolina, Charleston 29425.

ABSTRACT

Matrix-assisted laser desorption ionization (MALDI) mass spectrometry has been used to obtain accurate molecular weight information for the integral membrane proteins bacteriorhodopsin and bovine rhodopsin desorbed from solubilized membrane preparations. Mass differences in the molecular weights measured for bleached and unbleached bacteriorhodopsin and rhodopsin indicate the removal of the retinal chromophores upon bleaching. The MALDI technique was also successful for determination of the major cleavage products obtained upon treatment of membrane bound rhodopsin with endoproteinase Asp-N and thermolysin. Our results indicate that the MALDI method is a useful means of obtaining accurate molecular weight information on hydrophobic proteins isolated in their native membranes.




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Copyright © 1992 by the Biophysical Society.