Characterization of two carnation petal prolyl 4 hydroxylases
✍ Scribed by Florina Vlad; Päivi Tiainen; Carolyn Owen; Thodhoraq Spano; Firas Bou Daher; Fatiha Oualid; Namik Ozer Senol; Daniela Vlad; Johanna Myllyharju; Panagiotis Kalaitzis
- Book ID
- 110903825
- Publisher
- John Wiley and Sons
- Year
- 2010
- Tongue
- English
- Weight
- 638 KB
- Volume
- 140
- Category
- Article
- ISSN
- 0031-9317
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Prolyl hydroxylase, which is responsible for the hydroxylation of peptidyl proline residues, has been isolated and purified from the green alga Chlarnydomonas reinhardii. The enzyme, which appears to be loosely associated with microsomal membranes, was released into solution by sonication in the pre
The mussel foot secretes a variety of unusual hydroxyprolinecontaining collagenous and noncollagenous proteins. Prolyl4-hydroxylase acting on one or more of the secreted proteins was isolated from the foot by using conventional gel filtration and ion exchange chromatography. M, of the intact enzyme