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. 1972 Aug;50(2):275–282. doi: 10.1104/pp.50.2.275

Isolation of an Enzyme System Which Will Catalyze the Glycosylation of Extensin 1

Arthur L Karr Jr a,2
PMCID: PMC366124  PMID: 16658156

Abstract

Enzymes which catalyze the glycosylation of the cell wall protein extensin using uridine diphosphate l-arabinose-14C as a substrate are present in a crude extract prepared from suspension cultured sycamore cells (Acer pseudoplatanus L.). This enzyme system sediments when the crude extract is subjected to centrifugation at 37000g. A base hydrolysate of the product contains a mixture of hydroxyproline-arabinosides which are electrophoretically and chromatographically identical to those obtained by hydrolysis of extensin isolated from the cell wall. The hydroxyproline-rich protein used as an acceptor in the glycosylation reactions is present in the particulate fraction. In addition, evidence is presented which indicates that hydroxyproline-rich tryptic peptides prepared from the cell wall can also be used as an acceptor by this enzyme system. The presence of Mg2+ or Mn2+ in the reaction mixture increases the enzyme-catalyzed incorporation of arabinose into extensin by about 1.4 times. About two-thirds of the product mixture is composed of arabinose-containing compounds which have not been identified. Some of these products appear to be hydroxyproline-glycosides which have not been previously reported.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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