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Literature summary for 1.14.11.2 extracted from

  • Berg, R.A.; Kedersha, N.L.; Guzman, N.A.
    Purification and partial characterization of the two nonidentical subunits of prolyl hydroxylase (1979), J. Biol. Chem., 254, 3111-3118.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Gallus gallus
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-
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Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein subunit alpha: contains 16 residues of mannose, 1 residue of galactose and at least 2 residues of N-acetylglucosamine, subunit beta: contains 2 residues of mannose and 3 residues of galactose Gallus gallus

Purification (Commentary)

Purification (Comment) Organism
isolation of subunits by ion exchange chromatography on DEAE-cellulose in 8 M urea Gallus gallus

Source Tissue

Source Tissue Comment Organism Textmining
embryo
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Gallus gallus
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Subunits

Subunits Comment Organism
tetramer alpha2 beta2, alpha: 64000, beta: 60000, ratio 1 to 1, SDS-PAGE Gallus gallus