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The Structure and Stability of Thermolysin

Authors: L H, Weaver; W R, Kester; L F, Ten Eyck; B W, Matthews;

The Structure and Stability of Thermolysin

Abstract

Thermolysin is an extracellular proteolytic enzyme isolated from Bacillus thermoproteolyticus (Endo, 1962). The enzyme is quite thermostable, retaining over half of its activity after being heated in an aqueous solution for an hour at 80°C, while at 65°C practically no inactivation occurs (Endo, 1962; Matsubara, 1967).

Related Organizations
Keywords

Protein Denaturation, Binding Sites, Hot Temperature, Protein Conformation, Thermolysin, Calcium, Edetic Acid

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selected citations
These citations are derived from selected sources.
This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Citations provided by BIP!
popularity
This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
BIP!Popularity provided by BIP!
influence
This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Influence provided by BIP!
impulse
This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.
BIP!Impulse provided by BIP!
20
Average
Top 10%
Top 10%
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