78088-29-6Relevant articles and documents
Biochemical characterisation and assessment of fibril-forming ability of collagens extracted from Bester sturgeon Huso huso × Acipenser ruthenus
Zhang, Xi,Ookawa, Mika,Tan, Yongkai,Ura, Kazuhiro,Adachi, Shinji,Takagi, Yasuaki
, p. 305 - 312 (2014)
Collagens purified from Bester sturgeon organs were characterised biochemically, and their fibril-forming abilities and fibril morphologies formed in vitro clarified. Yields of collagens were 2.1%, 11.9%, 0.4%, 18.1%, 0.4%, 0.8% and 0.03% (collagen dry weight/tissue wet weight) from scales, skin, muscle, swim bladder, digestive tract, notochord and snout cartilage, respectively. Using SDS-PAGE and amino acid composition analyses, collagens from scales, skin, muscle, the swim bladder and digestive tract were characterised as type I, and collagens from the notochord and snout cartilage as type II. Denaturation temperatures of the collagens, measured using circular dichroism, were 29.6, 26.8, 29.0, 32.9, 31.6 and 36.3 °C in scales, skin, muscle, swim bladder, digestive tract, and notochord, respectively. For fibril formation, swim bladder and skin collagen showed a more rapid rate of increase in turbidity, a shorter time to attain the maximum turbidity, and formed thicker fibrils compared with porcine tendon type I collagen.
The 2-Oxoglutarate-Dependent Oxygenase JMJD6 Catalyses Oxidation of Lysine Residues to give 5S-Hydroxylysine Residues
Mantri, Monica,Loik, Nikita D.,Hamed, Refaat B.,Claridge, Timothy D. W.,McCullagh, James S. O.,Schofield, Christopher J.
experimental part, p. 531 - 534 (2012/01/12)
Amino acid analyses reveal that JMJD6-catalysed hydroxylation of RNA-splicing regulatory protein fragments occurs to give hydroxylysine products with 5S stereochemistry. This contrasts with collagen lysyl hydroxylases, which give 5R-hydroxylated products. The work suggests that more than one subfamily of lysyl hydroxylases has evolved and illustrates the importance of stereochemical assignments in proteomic analyses.
Stereoselective synthesis of (2R,5R)- and (2S,5R)-5-hydroxylysine
Van Den Nieuwendijk, Adrianus M. C. H.,Kriek, Nicole M. A. J.,Brussee, Johannes,Van Boom, Jacques H.,Van Der Gen, Arne
, p. 3683 - 3691 (2007/10/03)
A stereoselective synthesis of (2S,5R)-5-hydroxylysine (1) and (2R,5R)-5-hydroxylysine (17), based on a concept involving Williams glycine template methodology and (R)-hydroxynitrile lyase for the introduction of chirality at the α-position and the side-chain, respectively, is described. This strategy offers an expeditious route towards orthogonally protected 5-hydroxylysines.