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Applications of electrospray mass spectrometry to studies on the structural properties of ribonuclease A and ribonuclease B
Author(s) -
Camilleri P.,
Haskins N. J.,
Rudd P. M.,
Saunders M. R.
Publication year - 1993
Publication title -
rapid communications in mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.528
H-Index - 136
eISSN - 1097-0231
pISSN - 0951-4198
DOI - 10.1002/rcm.1290070505
Subject(s) - chemistry , ribonuclease , electrospray mass spectrometry , mass spectrometry , electrospray , ribonuclease iii , protein mass spectrometry , chromatography , s tag , ribonuclease t1 , electrospray ionization , biochemistry , rna , rnase p , rna interference , gene
Deuterium‐exchange experiments were performed on ribonuclease A (RNase A) and its glycosylated form, ribonuclease B (RNase B), using electrospray ionization mass spectrometry. The number of exchangeable protons was found to be similar for both forms of the enzyme, indicating that the oligosaccharide moiety on RNase B does not exert any influence on protein conformation. Four main glycoform populations were identified in RNase B, each of which was homogeneous and associated with one phosphate group. Spectra for RNase A were heterogeneous due to the presence of 0–3 phosphate groups bound to the enzyme.