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Biochemical characterization of the plasma membrane H/sup +/ - ATPase from red beet (Beta vulgaris) hypocotyl tissue

Thesis/Dissertation ·
OSTI ID:6592051
Several biochemical techniques including selective solubilization followed by gel filtration or various types of affinity chromatography, and antibody production were employed in an attempt to purify the plasma membrane H/sup +/ - ATPase from red beet hypocotyl tissue. While the enzyme could not be purified using any of these methods, it was possible to successfully conduct a more detailed biochemical analysis of the H/sup +/ - ATPase. The molecular weight and isoelectric point of the enzyme were determined using N,N'dicyclohexylcarbodiimide (DCCD) and a H/sup +/ - ATPase antibody. When plasma membrane vesicles were incubated with 20 ..mu..M (/sup 14/C)-DCCD at 0 C, a single 97,000 dalton protein was apparent on a fluorograph. A close correlation between (/sup 14/C)-DCCD labelling of the 97,000 dalton protein and the extent of ATPase inhibition over a range of DCCD concentrations suggests that this 97,000 dalton protein is a component of the plasma membrane H/sup +/ - ATPase. An antibody raised against the plasma membrane H/sup +/ - ATPase of Neurospora crassa cross-reacted with the 97,000 dalton DCCD-binding protein, further supporting the identity of this protein. Immunoblots of two dimensional gels of red beet plasma membrane vesicles indicated the isoelectric point of the enzyme to be pH 6.5.
Research Organization:
California Univ., Davis (USA)
OSTI ID:
6592051
Country of Publication:
United States
Language:
English