In:
FEBS Letters, Wiley, Vol. 164, No. 1 ( 1983-11-28), p. 67-70
Abstract:
Spinach chloroplasts are known to contain calmodulin and to display an envelope‐bound ATPase activity. This activity, stimulated by 0.15 mM Ca 2+ and 5 mM Mg 2+ , is further enhanced by calmodulin. The apparent K m for ATP was 0.55 mM. The enzyme was especially sensitive to NH 4 VO 3 , SbCl 3 , LaCl 3 and oligomycin. An attempt to isolate the ATPase by calmodulin‐Sepharose affinity chromatography was successful. The EGTA‐eluted fraction contained 2 proteins out of the 21 proteins separated previously by isoelectric focussing [(1983) Biochim. Acta 722, 226—333] and exhibited an ATPase activity.
Type of Medium:
Online Resource
ISSN:
0014-5793
,
1873-3468
DOI:
10.1016/0014-5793(83)80020-9
Language:
English
Publisher:
Wiley
Publication Date:
1983
detail.hit.zdb_id:
1460391-3
SSG:
12
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