Access the full text.
Sign up today, get DeepDyve free for 14 days.
J. Gilder, J. Cronshaw (1974)
A BIOCHEMICAL AND CYTOCHEMICAL STUDY OF ADENOSINE TRIPHOSPHATASE ACTIVITY IN THE PHLOEM OF NICOTIAN A TABACUMThe Journal of Cell Biology, 60
L. Tice (1969)
LEAD-ADENOSINE TRIPHOSPHATE COMPLEXES IN ADENOSINE TRIPHOSPHATASE HISTOCHEMISTRYJournal of Histochemistry and Cytochemistry, 17
M. Wachstein, E. Meisel (1957)
Histochemistry of hepatic phosphatases of a physiologic pH; with special reference to the demonstration of bile canaliculi.American journal of clinical pathology, 27 1
R. Serrano (1985)
Plasma membrane ATPase of plants and fungi
R. Serrano, M. Kielland-Brandt, G. Fink (1986)
Yeast plasma membrane ATPase is essential for growth and has homology with (Na+ + K+), K+- and Ca2+-ATPasesNature, 319
B. Bowman, F. Blasco, C. Slayman (1981)
Purification and characterization of the plasma membrane ATPase of Neurospora crassa.The Journal of biological chemistry, 256 23
G. Anthon, R. Spanswick (1986)
Purification and properties of the h-translocating ATPase from the plasma membrane of tomato roots.Plant physiology, 81 4
Van Alstine, J. Melvin (1984)
Cell partition in aqueous polymer two phase systems
F. Vara, R. Serrano (1982)
Partial purification and properties of the proton-translocating ATPase of plant plasma membranes.The Journal of biological chemistry, 257 21
F. Vara, R. Serrano (1981)
Purification and characterization of a membrane-bound ATP diphosphohydrolase from Cicer arietinum (chick-pea)roots.The Biochemical journal, 197 3
Abstract Cytochemical techniques employing lead-precipitation of enzymically released inorganic phosphate have been widely used in attempts to localize the plasma membrane proton pump (H+-ATPase) in electron micrographs. Using Avena sativa root tissue we have performed a side-by-side comparison of ATPase activity observed in electron micrographs with that observed in in vitro assays using ATPases found in the soluble and plasma membrane fractions of homogenates. Cytochemical analysis of oat roots, which had been fixed in glutaraldehyde in order to preserve subcellular structures, identifies an ATPase located at or near the plasma membrane. However, the substrate specificity and inhibitor sensitivity of the in situ localized ATPase appear identical to those of an in vitro ATPase activity found in the soluble fraction, and are completely unlike those of the plasma membrane proton pump. Further studies demonstrated that the plasma membrane H+-ATPase is particularly sensitive to inactivation by the fixatives glutaraldehyde and formaldehyde and by lead. In contrast, the predominant soluble ATPase activity in oat root homogenates is less sensitive to fixation and is completely insensitive to lead. Based on these results, we propose a set of criteria for evaluating whether a cytochemically localized ATPase activity is, in fact, due to the plasma membrane proton pump. 1 Supported by grants to M. R. S. from the Department of Energy (No. DE-AC0283ER13086) and to the College of Agriculture and Life Sciences (Hatch Project No. 1757) and to R. R. E. from the National Science Foundation (No. PCM 83-12442). This content is only available as a PDF. © 1988 American Society of Plant Biologists This article is published and distributed under the terms of the Oxford University Press, Standard Journals Publication Model (https://academic.oup.com/journals/pages/open_access/funder_policies/chorus/standard_publication_model)
Plant Physiology – Oxford University Press
Published: Mar 1, 1988
Read and print from thousands of top scholarly journals.
Already have an account? Log in
Bookmark this article. You can see your Bookmarks on your DeepDyve Library.
To save an article, log in first, or sign up for a DeepDyve account if you don’t already have one.
Copy and paste the desired citation format or use the link below to download a file formatted for EndNote
Access the full text.
Sign up today, get DeepDyve free for 14 days.
All DeepDyve websites use cookies to improve your online experience. They were placed on your computer when you launched this website. You can change your cookie settings through your browser.