Abstract
The p1mm membrane ATP-phosphohydrolm (ATPae) frm red beet (Bta swirb L) storge tissue wasol d ith the zwitterionic eter t Zittergea 3-14 from a plas membne-enriched fion which e with the aok det t, sodium deoxycholate. For both the extraction of ext s pe by deoxycholate awl the soublo t of active plasm membrane ATPase by Zw tteg 3-14, the op l co rtin ofd nt was 0.1% (weigt per vome) with a dett to protein ratio of 1.0(per). The of the solublUzed ATPase were fonnd to be similar to the mebrane-bomd enyme wit respect to pH oium, subtrate specificity, ibitor sensitivity, an kietics of K+ stimulation. The solubiHzed ATPase pretio formed a rapidly uring over phospbheyme, the bradW veloiy of whic wa as in the presene of 50 millimolr KC. So2b Mtonwith 0.1% Zwtergent 3-14 fohowig extation with 0.1% deoxycolate resulted in an inem in both ATPae activity and steady sate pbospboenzyne level; however, a direct correspnee betwee the increas in ATPase tivity and pLhospborylatio lvel did nt exist. It Is that this diepacy may be the result of a deternt-m ated m ctIon of kinetic rate consats in the mechanism of the enzyme.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 26-30 |
| Number of pages | 5 |
| Journal | Plant physiology |
| Volume | 76 |
| Issue number | 1 |
| DOIs | |
| State | Published - Jan 1 1984 |
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ASJC Scopus subject areas
- Physiology
- Genetics
- Plant Science
Cite this
Characterization of the solubilized plasma membrane ATPase of red beet. / Briskin, Donald P.; Poole, Ronald J.
In: Plant physiology, Vol. 76, No. 1, 01.01.1984, p. 26-30.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Characterization of the solubilized plasma membrane ATPase of red beet
AU - Briskin, Donald P.
AU - Poole, Ronald J.
PY - 1984/1/1
Y1 - 1984/1/1
N2 - The p1mm membrane ATP-phosphohydrolm (ATPae) frm red beet (Bta swirb L) storge tissue wasol d ith the zwitterionic eter t Zittergea 3-14 from a plas membne-enriched fion which e with the aok det t, sodium deoxycholate. For both the extraction of ext s pe by deoxycholate awl the soublo t of active plasm membrane ATPase by Zw tteg 3-14, the op l co rtin ofd nt was 0.1% (weigt per vome) with a dett to protein ratio of 1.0(per). The of the solublUzed ATPase were fonnd to be similar to the mebrane-bomd enyme wit respect to pH oium, subtrate specificity, ibitor sensitivity, an kietics of K+ stimulation. The solubiHzed ATPase pretio formed a rapidly uring over phospbheyme, the bradW veloiy of whic wa as in the presene of 50 millimolr KC. So2b Mtonwith 0.1% Zwtergent 3-14 fohowig extation with 0.1% deoxycolate resulted in an inem in both ATPae activity and steady sate pbospboenzyne level; however, a direct correspnee betwee the increas in ATPase tivity and pLhospborylatio lvel did nt exist. It Is that this diepacy may be the result of a deternt-m ated m ctIon of kinetic rate consats in the mechanism of the enzyme.
AB - The p1mm membrane ATP-phosphohydrolm (ATPae) frm red beet (Bta swirb L) storge tissue wasol d ith the zwitterionic eter t Zittergea 3-14 from a plas membne-enriched fion which e with the aok det t, sodium deoxycholate. For both the extraction of ext s pe by deoxycholate awl the soublo t of active plasm membrane ATPase by Zw tteg 3-14, the op l co rtin ofd nt was 0.1% (weigt per vome) with a dett to protein ratio of 1.0(per). The of the solublUzed ATPase were fonnd to be similar to the mebrane-bomd enyme wit respect to pH oium, subtrate specificity, ibitor sensitivity, an kietics of K+ stimulation. The solubiHzed ATPase pretio formed a rapidly uring over phospbheyme, the bradW veloiy of whic wa as in the presene of 50 millimolr KC. So2b Mtonwith 0.1% Zwtergent 3-14 fohowig extation with 0.1% deoxycolate resulted in an inem in both ATPae activity and steady sate pbospboenzyne level; however, a direct correspnee betwee the increas in ATPase tivity and pLhospborylatio lvel did nt exist. It Is that this diepacy may be the result of a deternt-m ated m ctIon of kinetic rate consats in the mechanism of the enzyme.
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UR - http://www.scopus.com/inward/citedby.url?scp=0038728485&partnerID=8YFLogxK
U2 - 10.1104/pp.76.1.26
DO - 10.1104/pp.76.1.26
M3 - Article
AN - SCOPUS:0038728485
VL - 76
SP - 26
EP - 30
JO - Plant Physiology
JF - Plant Physiology
SN - 0032-0889
IS - 1
ER -