serine protease

It was also described as having some serine protease activity.

For more on how this is accomplished, see serine protease.

There are at least 14 families of serine protease.

Like many other coagulation factors, it is a serine protease.

This gene encodes a member of the serine protease family.

This may have different consequences, depending on the normal function of the serine protease.

The enzymatic mechanism is similar to that of other serine proteases.

It is an enzyme of the serine protease class.

However, close relatives of chymotrypsin-like serine proteases are absent in plants.

DPP-4 is a serine protease located on the cell surfaces throughout the body.

It is then normally cleaved by a calcium independent serine protease.

Host organisms must ensure that the activity of serine proteases is adequately regulated.

Plasmin, like trypsin, belongs to the family of serine proteases.

All signal peptidases described so far are serine proteases.

The protein is a member of the intra membranous serine proteases.

This mode of catalysis is found in many enzymes, such as the serine proteases.

Drotrecogin alpha (activated) belongs to the class of serine proteases.

All members of the chymotrypsin family of serine proteases have very similar structures.

Determination of serine protease levels may be useful in the context of particular diseases.

Since its discovery in 1967, serine protease DPP-4 has been a popular subject of research.

Serine proteases are a common type of protease.

In addition, our data indicate that simply coating beads with any serine protease is not sufficient to influence migration.

The subtilisin family is the second largest serine protease family characterised to date.

However, it has sequence similarity with proteins tentatively annotated as serine proteases.

The gene is part of a cluster of serine protease genes on chromosome 16.