Assignment of disulfide bonds in proteins by partial acid hydrolysis and mass spectrometry

1990 ◽  
Vol 9 (5) ◽  
pp. 523-532 ◽  
Author(s):  
Zhongrui Zhou ◽  
David L. Smith
Keyword(s):  
Mass Spectrometry ◽  
Acid Hydrolysis ◽  
Disulfide Bonds ◽  
Partial Acid Hydrolysis

LOCATION OF DISULFIDE BONDS IN PROTEINS BY PARTIAL ACID HYDROLYSIS AND MASS SPECTROMETRY

1989 ◽  
pp. 176-185 ◽  
Author(s):  
Yiping Sun ◽  
Zhongrui Zhou ◽  
David L. Smith
Keyword(s):  
Mass Spectrometry ◽  
Acid Hydrolysis ◽  
Disulfide Bonds ◽  
Partial Acid Hydrolysis

Characterization of oligosaccharide moieties of intact glycoproteins by microwave-assisted partial acid hydrolysis and mass spectrometry

2005 ◽  
Vol 19 (18) ◽  
pp. 2553-2559 ◽  
Author(s):  
Bao-Shiang Lee ◽  
Sangeeth Krishnanchettiar ◽  
Syed Salman Lateef ◽  
Nabila Salman Lateef ◽  
Shalini Gupta
Keyword(s):  
Mass Spectrometry ◽  
Acid Hydrolysis ◽  
Partial Acid Hydrolysis ◽  
Microwave Assisted

scholarly journals C-terminal sequencing of protein. A novel partial acid hydrolysis and analysis by mass spectrometry

1992 ◽  
Vol 206 (3) ◽  
pp. 691-696 ◽  
Author(s):  
Akira TSUGITA ◽  
Keiji TAKAMOTO ◽  
Masaharu KAMO ◽  
Hiromoto IWADATE
Keyword(s):  
Mass Spectrometry ◽  
Acid Hydrolysis ◽  
Protein A ◽  
Partial Acid Hydrolysis

Towards the Standard-Module Approach to Disulfide-Linked Polypeptide Nanostructures. I. Methodological Prerequisites and Mass Spectrometric Characterization of the Test Two-Loop Structure

2003 ◽  
Vol 9 (2) ◽  
pp. 139-148 ◽  
Author(s):  
O.A. Mirgorodskaya ◽  
K.F. Haselmann ◽  
F. Kjeldsen ◽  
R.A. Zubarev ◽  
P. Roepstorff
Keyword(s):  
Mass Spectrometry ◽  
Disulfide Bonds ◽  
Bond Cleavage ◽  
Bond Formation ◽  
Peptide Bond ◽  
Biologically Active ◽  
Loop Structure ◽  
Partial Acid Hydrolysis ◽  
Peptide Bond Cleavage

Potentially biologically-active nanostructures can be created from single chains of unmodified peptides by cross-linking different regions of the chain by disulfide bonds and cleaving the chain at specified sites to obtain the final configuration. The availability of techniques for assembly and characterization of such structures was tested on a two-loop structure created from a 21-residue linear peptide. Directed intra-molecular disulfide bond formation was performed by inserting partial sequences favoring intra-molecular S–S bond formation (“loops”) separated by partial sequences disfavoring such a process (“spacers”) into the precursor sequence. Peptide bond cleavage by partial acid hydrolysis at specific sites (GG, NP/DP) inside the loops opened them; the same process in the spacer separated the loops. Synthesis, oxidation and bond cleavage were monitored by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI ToF MS). The hydrolysis fragments of the produced nanostructures were characterized by tandem electrospray ionization Fourier transform mass spectrometry (ESI FT-MS) with collisional and electron capture dissociations. The latter technique was especially useful as it cleaves S–S bonds preferentially. The feasibility of the proposed synthesis approach and the adequacy of the analysis techniques for the test structure were demonstrated.

Structural Analyses of Carbohydrate Moieties of Glycoproteins by Microwave-Assisted Partial Acid Hydrolysis and Mass Spectrometry

2008 ◽  
Vol 4 (1) ◽  
pp. 26-39 ◽  
Author(s):  
Bao-Shiang Lee ◽  
Sangeeth Krishnanchettiar ◽  
G. Lasanthi P. Jayathilaka ◽  
Syed Lateef ◽  
Shalini Gupta
Keyword(s):  
Mass Spectrometry ◽  
Acid Hydrolysis ◽  
Partial Acid Hydrolysis ◽  
Microwave Assisted

Oligosaccharide analyses of glycopeptides of horseradish peroxidase by thermal-assisted partial acid hydrolysis and mass spectrometry

2005 ◽  
Vol 340 (11) ◽  
pp. 1859-1865 ◽  
Author(s):  
Bao-Shiang Lee ◽  
Sangeeth Krisnanchettiar ◽  
Syed Salman Lateef ◽  
Nabila Salman Lateef ◽  
Shalini Gupta
Keyword(s):  
Mass Spectrometry ◽  
Horseradish Peroxidase ◽  
Acid Hydrolysis ◽  
Partial Acid Hydrolysis
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