High affinity binding of an N-terminal myristoylated p60 peptide

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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...

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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 degradation. ...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1989

ISSN: 0021-9258

DOI: 10.1016/s0021-9258(19)84805-6