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rdf:type | |
lifeskim:mentions | |
pubmed:dateCreated |
1992-7-13
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pubmed:abstractText |
In immunobiochemical blots, polyclonal antibodies against subunits of plant and mammalian vacuolar-type ATPases (V-ATPases) cross-react strongly with corresponding subunits of larval Manduca sexta midgut plasma membrane V-ATPase. Thus, rabbit antiserum against Kalanchoe daigremontiana tonoplast V-ATPase holoenzyme cross-reacts with the 67, 56, 40, 28 and 20 kDa subunits of midgut V-ATPase separated by SDS-PAGE. Antisera against bovine chromaffin granule 72 and 39 kDa V-ATPase subunits cross-react with the corresponding 67 and 43 kDa subunits of midgut V-ATPase. Antisera against the 57 kDa subunit of both beet root and oat root V-ATPase cross-react strongly with the midgut 56 kDa V-ATPase subunit. In immunocytochemical light micrographs, antiserum against the beet root 57 kDa V-ATPase subunit labels the goblet cell apical membrane of both posterior and anterior midgut in freeze-substituted and fixed sections. The plant antiserum also labels the apical brush-border plasma membrane of Malpighian tubules. The ability of antibodies against plant V-ATPase to label these insect membranes suggests a high sequence homology between V-ATPases from plants and insects. Both of the antibody-labelled insect membranes transport K+ and both membranes possess F1-like particles, portasomes, on their cytoplasmic surfaces. This immunolabelling by xenic V-ATPase antisera of two insect cation-transporting membranes suggests that the portasomes on these membranes may be V-ATPase particles, similar to those reported on V-ATPase-containing vacuolar membranes from various sources.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0022-0949
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
166
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
131-43
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:1534830-Adenosine Triphosphatases,
pubmed-meshheading:1534830-Animals,
pubmed-meshheading:1534830-Antibodies,
pubmed-meshheading:1534830-Biological Transport, Active,
pubmed-meshheading:1534830-Cations,
pubmed-meshheading:1534830-Cattle,
pubmed-meshheading:1534830-Cell Membrane,
pubmed-meshheading:1534830-Chromaffin System,
pubmed-meshheading:1534830-Cross Reactions,
pubmed-meshheading:1534830-Digestive System,
pubmed-meshheading:1534830-Immunochemistry,
pubmed-meshheading:1534830-Malpighian Tubules,
pubmed-meshheading:1534830-Moths,
pubmed-meshheading:1534830-Plants,
pubmed-meshheading:1534830-Species Specificity,
pubmed-meshheading:1534830-Vacuoles
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pubmed:year |
1992
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pubmed:articleTitle |
Antibodies to mammalian and plant V-ATPases cross react with the V-ATPase of insect cation-transporting plasma membranes.
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pubmed:affiliation |
Department of Entomology, Purdue University, West Lafayette, IN 47907.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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