Publication | Closed Access
Studies on the Primary Structure of Cow χ‐Casein.‐Structural Features of para‐χ‐Casein; N‐terminal sequence of χ‐caseinoglycopeptide studied with a sequencer
27
Citations
14
References
1972
Year
Peptide EngineeringGlycobiologyMolecular BiologyPeptide SciencePeptide TherapeuticsPeptide ChemistryN‐terminal SequenceChemical BiologyCow χ‐Casein.‐structural FeaturesProtein FoldingProtein X-ray CrystallographyProtein ChemistrySeveral Tryptic PeptidesBiochemistryStructural BiologyTryptic PeptidesPrimary StructureNatural SciencesPeptide LibraryPeptide TherapeuticPeptide SynthesisChymotryptic Overlap PeptidesMedicine
Abstract Several long tryptic peptides obtained from reduced maleylated χ‐casein were sequenced: they belonged to the N‐ and C‐terminal (37 residues) moieties of para‐χ‐casein. Several tryptic peptides could then be joined by chymotryptic overlap peptides. 102 amino acid residues of para‐χ‐casein were thus placed into two long and four shorter sequences. Some structural results were established with a Sequencer which was also employed for a verification of the N‐terminal sequence of the χ‐caseinoglycopeptide; a previously described short glycopeptide was found again and was reinvestigated.
| Year | Citations | |
|---|---|---|
Page 1
Page 1