What activates chymotrypsinogen?

It is trypsin that activates chymotrypsinogen.

Trypsin is a type of protease, EC, which is from the pancreas of cattle, sheep and pigs.

An extraction of a serine proteolytic enzyme. in vertebrates.

, as a digestive enzyme.

After trypsinogen, the pancreas is the precursor of trypsin, it is secreted as a component of pancreatic juice and is decomposed into activated trypsin by enterokinase or trypsin, which is an endonuclease that can take lysine in the polypeptide chain.

and carboxyl groups in arginine residues.

Side cut-off. It not only plays the role of digestive enzymes, but also restricts the decomposition of the precursors of other enzymes such as chymotrypsinogen, carboxypeptidase, phospholipidase and other enzymes, and plays an activation role. It is the most specific protease and determines the amino acids of proteins.

In arrangement, it becomes an indispensable tool.

It is trypsin that activates chymotrypsinogen. Trypsin can activate chymotrypsin to chymotrypsin, and can quickly activate the rest of the large amount of trypsinogen to trypsin.

Trypsin and chymotrypsin work together on proteins, which are broken down into peptides and a small amount of amino acids. Pancreatic amylase and a small amount of pancreatic maltase present in pancreatic juice can promote the decomposition of starch and maltose into glucose, respectively. Pancreatic lipase, with the synergistic effect of bile, promotes the breakdown of fat into fatty acids and glycerol.

To be precise, it is the trypsinogen that has been activated, so choose B

It is trypsin that activates chymotrypsinogen.

Trypsin is a type of protease, EC, is a serine proteolytic enzyme extracted from the pancreas of cattle, sheep and pigs. In vertebrates, it functions as a digestive enzyme.

After trypsinogen, the precursor of trypsin, the pancreas is synthesized, it is secreted as a component of pancreatic juice, and is decomposed into activated trypsin by intestinal kinase, or trypsin, which is an endonuclease that can cut off the carboxyl side of lysine and arginine residues in the polypeptide chain.

It not only plays the role of digestive enzymes, but also restricts the decomposition of the precursors of other enzymes such as chymotrypsinogen, carboxypeptidase, phospholipidase and other enzymes, and plays an activation role. It is the most specific protease, and it has become an indispensable tool in determining the amino acid arrangement of protein cryptology.

Answer]: B Analysis: Myrutogen is converted into active chymotrypsin under the action of trypsin. Trypsinogen is activated by intestinal inactivating enzymes in intestinal fluid to become active trypsin.

The activation of chymotrypsin Lao Hengyuan depends on:

a.Bicarbonate.

b.Hydrochloric acid. c.Trypsin.

d.Enteroactivating enzymes.

e.Tissue fluid.

Correctly answer the case containing silver: c

Activation of chymotrypsinogen is dependent on (coarse years).

a.Trypsin.

d.Enterokinase bench pure.

e.Tissue fluid.

Correct Answer: a

Answer]: c can make trypsinogen into trypsin There are many substances, such as enterokinase, gastric acid, pancreatic egg white enzyme itself and tissue fluid, among which enterokinase is the most important. Tryptanogen activates to trypsin, which activates chymotrynogen to chymotrypsin.

Pepsinogen can be activated as a pepin enzyme under the action of gastric acid.

Answer: B

Trypsinogen is converted into trypsin by intestinal activating enzymes, which in turn activates chymotrypsin or chymogen, which is converted into chymotrypsin.

Activation of myrosinase protangerine refers to ().

a.Enterokinase.

b.Salt round cavity with acid.

c.Tissue fluid.

d.Trypsin.

e.Colipase.

Correct answer: d