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Tonoplast and plasma membrane ATPases from maize lines of high or low vigour

Published online by Cambridge University Press:  19 September 2008

S. Sánchez-Nieto
Affiliation:
Depto de Bioquímica, División de Estudios de Posgrado, Facultad de Química, Edificio E Universidad Nacional Autónoma de México, Ciudad Universitaria, 04510 México, D. F.México
R. Rodríguez-Sotres
Affiliation:
Depto de Bioquímica, División de Estudios de Posgrado, Facultad de Química, Edificio E Universidad Nacional Autónoma de México, Ciudad Universitaria, 04510 México, D. F.México
P. González-Romo
Affiliation:
Depto de Bioquímica, División de Estudios de Posgrado, Facultad de Química, Edificio E Universidad Nacional Autónoma de México, Ciudad Universitaria, 04510 México, D. F.México
I. Bernal-Lugo
Affiliation:
Depto de Bioquímica, División de Estudios de Posgrado, Facultad de Química, Edificio E Universidad Nacional Autónoma de México, Ciudad Universitaria, 04510 México, D. F.México
M. Gavilanes-Ruíz*
Affiliation:
Depto de Bioquímica, División de Estudios de Posgrado, Facultad de Química, Edificio E Universidad Nacional Autónoma de México, Ciudad Universitaria, 04510 México, D. F.México
*
* Correspondence

Abstract

The effectiveness of ATPase in germinated seed may play an important role in the vigour of germination. The activities of tonoplast and plasma membrane ATPases in two maize (Zea mays L.) lines with different vigour of germination were determined. ATP hydrolysis was measured in microsomal fractions from coleoptiles along with the responses to specific inhibitors for the plasma membrane, tonoplast and mitochondrial ATPases as well as for acid phosphatase. Nitrate-sensitive ATPase activity was 1.5–3.0 times lower in the low-vigour line than in the high-vigour line. Kinetic analysis of ATP hydrolysis at different substrate concentrations revealed the existence of two enzymes in the microsomal fractions of the two lines. The Vmax of enzyme 1 in the low-vigour line was a third of that in the high-vigour line. This enzyme was identified as the nitrate-sensitive or tonoplast ATPase on the basis of measurements of ATP hydrolysis in the presence of specific inhibitors at high (8.12mm) and low (0.77mm) ATP concentrations.

Type
Research Papers
Copyright
Copyright © Cambridge University Press 1992

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