Isolation of an enzyme system which will catalyze the glycosylation of extensin.

Plant Physiology
A L Karr

Abstract

Enzymes which catalyze the glycosylation of the cell wall protein extensin using uridine diphosphate l-arabinose-(14)C 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 Mg(2+) or Mn(2+) 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.

References

Jan 1, 1967·Proceedings of the National Academy of Sciences of the United States of America·J Holleman
Jul 18, 1969·Science·D Sadava, M J Chrispeels
Nov 19, 1960·Nature·S J KOLLAR, M JARAI
Jan 1, 1964·Experimental Cell Research·D T LAMPORT
Sep 9, 1950·Nature·W E TREVELYANJ S HARRISON
Oct 1, 1969·Proceedings of the National Academy of Sciences of the United States of America·P M RayM M Ray
Oct 1, 1971·Plant Physiology·D T Lamport, D H Miller

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