Collagens are among proteins that undergo several post-translational modifications, such as prolyl hydroxylation, that occur during elongation of the nascent chains in the endoplasmic reticulum. The major structural collagens, types I, II and III, have large, uninterrupted triple helices, comprising
Nihon eiseigaku zasshi. Japanese journal of hygiene, 49(4), 797-806 (1994-10-01)
to observe the influence of aging on urinary secretion of 3-hydroxyproline (3-Hyp) in normal subjects and in cancer patients and study the effects of aging on the accuracy of urinary 3-Hyp as a general-purpose cancer screening test. We reanalyzed, from
A new rapid method for quantitating radioactive proline, 4-hydroxyproline, and 3-hydroxyproline.
Proline residues in collagens are extensively hydroxylated post-translationally. A rare form of this modification, (3S,2S)-l-hydroxyproline (3Hyp), remains without a clear function. Disruption of the enzyme complex responsible for prolyl 3-hydroxylation results in severe forms of recessive osteogenesis imperfecta (OI). These
Identification of 3-hydroxyproline residues in several proteins of Fasciola hepatica.
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