Reconstitution of adenosine triphosphatase of thermophilic bacterium from purified individual subunits.

Explore this paper's citation graph

Summary

The ATPase activity reconstituted from alpha + beta + delta was thermolabile and insensitive to NaN3, whereas the activities obtained from mixtures containing beta and gamma were thermostable and sensitive to NaNs3, like the native ATPase.

Type
article
Published
1977-05-25
Cited by
145
References
0
Access
Open access

Keywords

Thermolabile, ATPase, BETA (programming language), Chemistry, Protein subunit

References

No references recorded for this paper.

Cited by

Related papers