Analysis of polymer surfaces by fast atom bombardment mass spectrometry.
نویسندگان
چکیده
منابع مشابه
FAST ATOM BOMBARDMENT MASS SPECTROMETRY (FABMS) ANALYSIS OF AN N- TERMINAL - BLOCKED PEPTIDE
FABMS analysis of T-lb peptide before and after one cycle of Edman degradation indicated an unblocked N-terminal Thr residue for this tryptic peptide. In contrast , our data showed a molecular protonated ion, MH + for T- la peptide at 655 mass units (mu) which is 42 mu higher than the MH ion of T- 1b peptide. In addition, T- la peptide was not amenable to one cycle of manual Edman degrada...
متن کاملFast - atom - bombardment mass spectrometry
A detailed study of the mass spectra of peptides produced by the new technique of fast-atom bombardment is reported. Molecular weights of unmodified peptides containing up to 21 amino acids have been determined. In favourable cases, the molecular-weight determination may be made on as little as 0.1 nmol of sample. Positive-ion and negative-ion spectra are obtained with equal facility. With samp...
متن کاملContinuous-flow fast atom bombardment mass spectrometry.
The continuous-flow fast atom bombardment probe performs equally well with or without a high-performance liquid chromatography column producing clean spectra containing little or no background noise. Its function as a liquid chromatography-mass spectrometry interface for labile and involatile samples has been illustrated with reference to dansylated amino acids. The versatility of the new probe...
متن کاملC-terminal peptide identification by fast atom bombardment mass spectrometry.
A previously described technique [Rose, Simona, Offord, Prior, Otto & Thatcher (1983) Biochem. J. 215, 273-277] permits the identification of the C-terminal peptide of a protein as the only peptide that does not incorporate any 18O upon partial enzymic hydrolysis in 18O-labelled water. Formation of chemical derivatives followed by combined g.l.c.-m.s. was used in this earlier work. We now descr...
متن کاملfast atom bombardment mass spectrometry (fabms) analysis of an n- terminal - blocked peptide
fabms analysis of t-lb peptide before and after one cycle of edman degradation indicated an unblocked n-terminal thr residue for this tryptic peptide. in contrast , our data showed a molecular protonated ion, mh + for t- la peptide at 655 mass units (mu) which is 42 mu higher than the mh ion of t- 1b peptide. in addition, t- la peptide was not amenable to one cycle of manual edman degradation. ...
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ژورنال
عنوان ژورنال: BUNSEKI KAGAKU
سال: 1991
ISSN: 0525-1931
DOI: 10.2116/bunsekikagaku.40.11_705