phospholipase

The release may be under the control of a phospholipase C.

This triggers the release of a phospholipase at the cell membrane.

Citicoline's effects may also be explained by the reduction of phospholipase A2 activity.

A high phospholipase A2 content may cause cardiotoxicity and myotoxicity.

This is thought to be induced by a specific protein phospholipase c zeta.

It also may inhibit phospholipase A as part of its mechanism of action.

Lecithinase is a type of phospholipase that acts upon lecithin.

The test measures the blood concentration of an enzyme called lipoprotein-associated phospholipase A2.

In addition, the following human proteins contain the phospholipase A2 domain:

The gene codes for the enzyme phospholipase C β2.

It is also attributed a minor role in activation of the phospholipase C pathway.

The hydrolysis is generally the result of the enzymatic action of phospholipase A2.

These proteins usually have phospholipase C as effector protein.

Influence of phospholipase A2 on human blood platelet α-adrenergic receptor function.

The gene encoding cytosolic phospholipase A2-α is found on chromosome 1.

Activation of these receptors activates the phospholipase C second messenger system.

The phospholipase travels to the nuclear membrane.

Its also known that this species' venom contains a "novel" phospholipase A with a strong anticoagulant activity.

The recommended name for the gene product is patatin-like phospholipase domain-containing protein 3.

The enzyme is called phospholipase A2 .

The prokaryotic phospholipase A2 domain is found in bacterial and fungal phospholipases.

Although the escape from the phagosome is not well understood, it is thought to be mediated by phospholipase A2 activity.

The pancreas also secretes phospholipase A2, lysophospholipase, and cholesterol esterase.

Phospholipase A1 is a phospholipase enzyme which removes the 1-acyl.

It bears similarity to its PLA2 family in phospholipase activity and calcium dependence.