Matrix-assisted laser desorption analysis of corticotropin-releasing factor-binding protein and activin by means of immunoprecipitation

A. Grey Craig; Steven W. Sutton; Joan Vaughan; Wolfgang H. Fischer

doi:10.1117/12.237633

1 April 1996 Matrix-assisted laser desorption analysis of corticotropin-releasing factor-binding protein and activin by means of immunoprecipitation

A. Grey Craig, Steven W. Sutton, Joan Vaughan, Wolfgang H. Fischer

Author Affiliations +

Proceedings Volume 2680, Ultrasensitive Biochemical Diagnostics; (1996) https://doi.org/10.1117/12.237633
Event: Photonics West '96, 1996, San Jose, CA, United States

Abstract

A sensitive immunoprecipitation procedure suitable for matrix assisted laser desorption mass spectrometry (MALD-MS) has been developed for the analysis of proteins. The ultimate goal of this work is to develop a method suitable for analysis of proteins from biological fluids such as plasma, serum and expression media at physiologically relevant concentrations. Proteins are specifically precipitated from complex mixtures by immunoprecipitation with antibodies directed against portions of the protein of interest and the immunoprecipitates are analyzed by MALD-MS. Here we show that the method is applicable to two proteins, the 35 kDa glycoprotein, corticotropin releasing factor-binding protein (CRF-BP) and the 26 kDa homodimeric protein, activin. In order to elucidate the constraints for achieving our ultimate goal we report MALD-MS experiments and parallel analyses with gel electrophoresis and immunostaining. Using this MALD-MS immunoprecipitation procedure we have been able to successfully analyze samples of CRF-BP or activin in the presence or absence of serum.

Citation Download Citation

A. Grey Craig, Steven W. Sutton, Joan Vaughan, and Wolfgang H. Fischer "Matrix-assisted laser desorption analysis of corticotropin-releasing factor-binding protein and activin by means of immunoprecipitation", Proc. SPIE 2680, Ultrasensitive Biochemical Diagnostics, (1 April 1996); https://doi.org/10.1117/12.237633

ACCESS THE FULL ARTICLE

INSTITUTIONAL
Select your institution to access the SPIE Digital Library.

SELECT YOUR INSTITUTION

PERSONAL
Sign in with your SPIE account to access your personal subscriptions or to use specific features such as save to my library, sign up for alerts, save searches, etc.

PERSONAL SIGN IN

No SPIE Account? Create one

PURCHASE THIS CONTENT

SUBSCRIBE TO DIGITAL LIBRARY

50 downloads per 1-year subscription

Members: $195

Non-members: $335 ADD TO CART

25 downloads per 1 - year subscription

Members: $145

Non-members: $250 ADD TO CART

PURCHASE SINGLE ARTICLE

Includes PDF, HTML & Video, when available