Abstract:
:The peptidyl prolyl hydroxylase responsible for the formation of hydroxyproline during arabinogalactan-protein biosynthesis in Lolium multiflorum (ryegrass) endosperm cells is a membrane-associated enzyme which will catalyze the hydroxylation of poly(l-proline) in the presence of oxygen, alpha-ketoglutarate, ferrous ion, and ascorbate. The K(m) for poly(l-proline) (8000 molecular weight) is 40 micromolar. The enzyme will also hydroxylate the protocollagen analog (Pro-Pro-Gly)(5).4H(2)O.Fractionation of membranes from protoplast lysates on a discontinuous sucrose/sorbitol density gradient, followed by centrifugation on a linear sucrose gradient in the presence of Mg(2+), leads to a clear separation of a number of membrane components. The membrane components have been tentatively identified using marker enzymes and assayed for peptidyl prolyl hydroxylase. It is concluded that the ryegrass prolyl hydroxylase is enriched in Golgi-derived membranes, but that significant amounts are also located in other subcellular fractions, including the rough endoplasmic reticulum.
journal_name
Plant Physioljournal_title
Plant physiologyauthors
Cohen PB,Schibeci A,Fincher GBdoi
10.1104/pp.72.3.754subject
Has Abstractpub_date
1983-07-01 00:00:00pages
754-8issue
3eissn
0032-0889issn
1532-2548journal_volume
72pub_type
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