Consequences of an altered antitrypsin level The increase in alpha-1-antitrypsin itself has hardly any negative consequences for the body and is a normal reaction to abnormal processes in the body. The change in value is therefore an indication of possibly pathological processes in the body, which in turn lead to symptoms of illness. In this … Consequences of an altered antitrypsin level | Alpha-1-antitrypsin
What is a tyrosine kinase? Tyrosine kinase is a specific group of enzymes that are functionally assigned to protein kinases in a biochemical sense. Protein kinases reversibly (possibility of back-reaction) transfer phosphate groups to the OH group (hydroxy group) of the amino acid tyrosine. The phosphate group is transferred to the hydroxy group of the … The tyrosine kinase
What is the tyrosine kinase receptor? The tyrosine kinase receptor represents a membrane-bound receptor, i.e. a receptor anchored in the cell membrane. Structurally, it is a receptor with a transmembrane complex. This means that the receptor passes through the entire cell membrane and also has an extra- and intracellular side. On the extracellular side, the … What is the tyrosine kinase receptor? | The tyrosine kinase
For which indications are they used? Tyrosine kinase inhibitors are used for various malignant diseases. Imatinib is used in particular in chronic myeloid leukemia. Further applications are non-small cell lung cancer (NSCLC), breast cancer and colon cancer. Due to the highly selective attack mechanism of tyrosine kinase inhibitors, they are generally better tolerated than conventional … For which indications are they used? | The tyrosine kinase
Introduction Trypsin is an enzyme that is produced in the pancreas and is very important for the digestion of humans. It activates other digestive enzymes from the pancreas in the intestine, which in turn further break down proteins that are taken in with food. These can then be absorbed by the intestine as it continues … Trypsin
Trypsin inhibitors Trypsin inhibitors are peptides that prevent trypsin from exerting its effect in the intestine or restrict it. Trypsin is blocked and cannot fulfil its function as an activator of other digestive enzymes in the intestine. Trypsin inhibitors are found in various foods. A well-known representative is soybeans, which contain trypsin inhibitors in raw … Trypsin inhibitors | Trypsin
At what pH value does Trypsin work best? Trypsin, like most other digestive enzymes, can only work properly at a certain pH. The optimal pH range for trypsin is between 7 and 8, which corresponds to the pH range in the small intestine of a healthy person. If this range changes, trypsin can no longer … At what pH value does Trypsin work best? | Trypsin
Definition – What is trypsinogen? Trypsinogen is the inactive precursor, a so-called proenzyme, of an enzyme that is produced in the pancreas. Together with the remaining pancreatic secretion, known as pancreatic saliva, the proenzyme trypsinogen is released via the pancreatic ducts into the duodenum, a part of the small intestine. This is where activation to … Trypsinogen
Where is trypsinogen produced? The proenzyme trypsinogen is roughly formulated in the pancreas. This lies transversely in the upper abdomen on the left side of the stomach. The pancreas can also be divided into two parts: The endocrine part produces hormones like insulin for the regulation of the sugar balance, which act within the body. … Where is trypsinogen produced? | Trypsinogen
Alpha-1-Antitrypsin Deficiency The cause of alpha-1-antitrypsin deficiency is often a genetic defect. Alpha-1-antitrypsin is an enzyme that inhibits other enzymes in their function. The enzymes that are inhibited normally have the task of breaking down proteins, which causes them to lose their function. Alpha-1-antitrypsin can therefore also be called a proteinase inhibitor. The enzymes that … Alpha-1-Antitrypsin Deficiency | Trypsinogen
