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A Protein Sequenator

European Journal of Biochemistry · 1967 · Vol. 1(1) · pp. 80–91
Pehr EdmanGeoffrey S. Begg

Abstract

The protein sequenator is an instrument for the automatic determination of amino acid sequences in proteins and peptides. It operates on the principle of the phenylisothiocyanate degradation scheme. The automated process embraces the formation of the phenylthiocarbamyl derivative of the protein and the splitting off of the N‐terminal amino acid as thiazolinone. The degradation proceeds at a rate of 15.4 cycles in 24 hours and with a yield in the individual cycle in excess of 98%. The material requirements are approximately 0.25 μmoles of protein. The thiazolinones are converted to the corresponding phenylthiohydantoins in a separate operation, and the latter identified by thin layer chromatography. The process has been applied to the whole molecule of apomyoglobin from the humpback whale, and it has been possible to establish the sequence of the first 60 amino acids from the N‐terminal end.

Cancer, Hypoxia, and MetabolismYield (engineering)Amino acidDegradation (telecommunications)ChemistryDerivative (finance)Sequence (biology)Amino acid residueChromatographyPeptide sequenceBiochemistry

MeSH terms

Amino Acid SequenceAnimalsBiochemistryCetaceaChromatography, Thin LayerIndicators and ReagentsThiocyanates

Funding

  • Medical Research Council
  • National Health and Medical Research Council
Citations
2,841
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References
Human fibrinopeptides isolation, characterization and structure
Biochimica et Biophysica Acta (BBA) - General Subjects · 1966 · 426 citations
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