Abstract:
:Metal-binding peptides in proteolytic digest maps have been identified by matrix-assisted UV laser desorption time-of-flight mass spectrometry (LDTOF-MS). The plasma and milk metal transport protein chosen to demonstrate this process, histidine-rich glycoprotein (HRG), was purified and then digested with trypsin; the cleavage products were analyzed by LDTOF-MS with dihydroxybenzoic acid as the matrix. The selective interaction of specific peptides with one or more Cu atoms was observed when Cu(II) ions were added to the digest mixture. At least one specific metal-binding peptide was identified by computerized sequence analysis using the molecular mass data and available cDNA sequence. These results demonstrate the first direct observation by mass spectrometry of differential peptide-metal ion interactions in protein digest maps. The ability to evaluate peptide-metal ion interactions, including stoichiometry, with less than 1 pmol of sample improves significantly our ability to identify metal binding domains in metal-binding proteins.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Hutchens TW,Nelson RW,Yip TTdoi
10.1016/0014-5793(92)80412-asubject
Has Abstractpub_date
1992-01-13 00:00:00pages
99-102issue
1eissn
0014-5793issn
1873-3468pii
0014-5793(92)80412-Ajournal_volume
296pub_type
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