Publication | Open Access
Comparative study of cow and sheep κ‐caseinoglycopeptides: Determination of the N‐terminal sequences with a sequencer and location of the sugars
34
Citations
11
References
1973
Year
N‐terminal SequencesGlycobiologyMolecular BiologyPolysaccharideRennin ClotringBiosynthesisProtein FoldingEaibohydrate GroupGlycosylationAnimal PhysiologyProtein ChemistryCasein RniccileBiochemistryAnimal NutritionSheep κ‐CaseinoglycopeptidesComparative StudyBiomolecular EngineeringAnimal ScienceNatural SciencesMedicineCarbohydrate-protein Interaction
K-Casein plays a major role in the stabilization of the casein rniccile in its natural etivironment 111 and in-the clotting phenomenon induced by t&action of rennin (EC 3.4.4.3); it' is also the only casein fraction hi cOIlti3iM sugars 12, 31, TO the hCtCXOgC&ty Of K-cascin from pooled milk are contributing the genetic variants, but also the non-identical composiPion of the carbohydrate groups present.This observation is in ~cordance with Cottschalk's [4] concept on the hetcrogtineity of the eaibohydrate group iti glyeopro-t&s_ During the rennin clotring of milk a. Phe-Met bond ,is split J5].A large peptide, called K-macropep-
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