Hostname: page-component-cd9895bd7-gbm5v Total loading time: 0 Render date: 2024-12-28T01:56:45.966Z Has data issue: false hasContentIssue false
  • English
  • Français

Purification and characterization of invertases from leaves of Lolium temulentum

Published online by Cambridge University Press:  01 February 1997

R. P. WALKER ,
A. L. WINTERS  and
C. J. POLLOCK
R. P. WALKER
Affiliation:
Institute of Grassland and Environmental Research, Plas Gogerddan, Aberystwyth, Dyfed SY23 3EB, UK
A. L. WINTERS
Affiliation:
Institute of Grassland and Environmental Research, Plas Gogerddan, Aberystwyth, Dyfed SY23 3EB, UK
C. J. POLLOCK
Affiliation:
Institute of Grassland and Environmental Research, Plas Gogerddan, Aberystwyth, Dyfed SY23 3EB, UK
Get access

Abstract

Leaves of Lolium temulentum L. contain both low and high pI acid invertases. Immunoblot analysis of a highly purified preparation of these forms suggested that they both possess a subunit molecular weight of 68 kDa. Protoplasts and their derived vacuoles were isolated from leaf blades and contained sufficient acid invertase activity to account for all the activity found in the soluble fraction of crude homogenates of leaf blades. Alkaline invertase was present in the basal region of leaves and, unlike acid invertase, did not bind to Con A-Sepharose, suggesting that the acid invertase was a glycoprotein and that the alkaline invertase was not. Fructose inhibited both acid and alkaline invertases. The hypothesis is discussed that activity in vivo could be modulated by the concentration of free fructose.

Keywords

Acid invertasealkaline invertaseLolium temulentumvacuole
Type
Research Article
Information
The New Phytologist , Volume 135 , Issue 2 , February 1997 , pp. 259 - 266
Copyright
Trustees of the New Phytologist 1997

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)