ISSN:
1438-2199
Schlagwort(e):
Amino acids
;
Cross-links
;
Peroxidases
;
Catechol oxidase
;
Glutamyl transferase
;
Lysyl oxidase
;
Resilin
;
Fibrin
;
Collagen
Quelle:
Springer Online Journal Archives 1860-2000
Thema:
Medizin
Notizen:
Summary The cross-linking of protein molecules to form stable supramolecular aggregates capable of acting as protective and supporting structures is a common feature of organisms coping with the stresses of life. These new polymeric forms range from thick rigid structures to thin flexible membranes. The formation of such cross-links must be carefully controlled since more or less than optimal cross-linking could lead to malfunction or even death of the organism. The chemistry of the amino acids converted or directly involved in the formation of these cross-links is complex and a range of new amino acids has been identified. Di- and tri-tyrosines are formed by the action of peroxidases, quinones by catechol oxidases,γ glutamyl lysine iso-peptide bonds by glutamyl transferase and a complex series of lysine- aldehyde derived cross-links induced by lysyl oxidase. These cross-linking mechanisms provide an insight into the complex changes in tissue function during growth of the organism and their effects on the properties of foods.
Materialart:
Digitale Medien
URL:
http://dx.doi.org/10.1007/BF00813999
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