MONITORING CLEAVAGE OF FUSION PROTEINS BY MATRIX-ASSISTED LASER-DESORPTION IONIZATION MASS-SPECTROMETRY - RECOMBINANT HIV-1 (IIIB) P26

Citation
Ce. Parker et al., MONITORING CLEAVAGE OF FUSION PROTEINS BY MATRIX-ASSISTED LASER-DESORPTION IONIZATION MASS-SPECTROMETRY - RECOMBINANT HIV-1 (IIIB) P26, Analytical biochemistry, 239(1), 1996, pp. 25-34
Citations number
21
Categorie Soggetti
Biology
Journal title
ISSN journal
00032697
Volume
239
Issue
1
Year of publication
1996
Pages
25 - 34
Database
ISI
SICI code
0003-2697(1996)239:1<25:MCOFPB>2.0.ZU;2-C
Abstract
Matrix-associated laser desorption ionization/mass spectrometry (MALDI /MS) has been used to examine whole bacteria for the presence of a rec ombinant HIV p26 fusion protein. MALDI/MS, combined with affinity-puri fication techniques, is also shown to be very useful in monitoring the enzymatic cleavage of both affinity-bound fusion protein and fusion p rotein in solution. The combination of mass resolution, sensitivity, a nd speed of analysis makes MALDI/MS an attractive alternative to SDS-P AGE. (C) 1995 Academic Press, Inc.