Analysis of the aliphatic 1H‐NMR spectrum of plasminogen kringle 4: A comparative study of human, porcine, bovine and chicken homologs

Andrew M. PETROS, Marianne GYENES, László PATTHY, Miguel LLINÁS

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Abstract

The aliphatic 1H‐NMR spectrum of the kringle 4 domain of human plasminogen has been studied via two‐dimensional chemical shift correlated (COSY) and nuclear Overhauser correlated (NOESY) experiments at 300 MHz and 620 MHz. A number of aliphatic proton spin systems have been identified and several definite assignments have been made. This was mainly achieved by comparison of the human kringle 4 spectrum with spectra of the porcine, bovine and chicken homologs and also with that of the kringle 1 from human plasminogen on which we have reported previously. The three valyl and two leucyl residues of human kringle 4 have been assigned. The eleven threonyl spin systems have been identified via a RELAYED‐COSY experiment and Thr17 has been assigned. The three alanyl spin systems have been identified and assigned. Six seryl spin systems have been identified and the signals from the seven glycyl residues of human kringle 4 have been located with Gly45 assigned. Furthermore, 24 AMX spin systems have been mapped in the COSY spectrum of human kringle 4 and Hα‐Hβ,β′ spin systems of Tyr2, Tyr41, Tyr50, Tyr74, Trp25 and Trp62 have been assigned. From the spectrum of a deglycosylated chicken homolog, the ɛ‐methyl singlets of Met28 and Met48 have been assigned. Finally, ligand effects on selected aliphatic resonances were observed which could be analyzed in terms of residues likely to neighbor the kringle lysine‐binding site.

Original languageEnglish
Pages (from-to)549-563
Number of pages15
JournalEuropean Journal of Biochemistry
Volume170
Issue number3
DOIs
Publication statusPublished - Jan 1988

ASJC Scopus subject areas

  • Biochemistry

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