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Isolation and characterization of prolyl hydroxylase fromChlamydomonas reinhardii

✍ Scribed by P. Blankenstein; W. C. Lang; D. G. Robinson

Book ID: 104752997
Publisher: Springer-Verlag
Year: 1986
Tongue: English
Weight: 910 KB
Volume: 169
Category: Article
ISSN: 0032-0935
DOI: 10.1007/bf00392320

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✦ Synopsis

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 presence of detergent. Purification was achieved by ion-exchange chromatography followed by affinity chromatography using the immobilized substrate poly-L-proline. Apart from its differing substrate specificity the enzyme appears to possess similar molecular characteristics to prolyl hydroxylase isolated from animal tissues: the active enzyme is a tetramer of about 240-250 kDa and nonidentical monomers of 65 and 60 kDa. The monomers are capsule shaped having a dimension of 12 x 7 nm.

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