This is a default text for your page Prince Ngoah/sandbox 1. Click above on edit this page to modify. Be careful with the < and > signs.
You may include any references to papers as in: the use of JSmol in Proteopedia [1] or to the article describing Jmol [2] to the rescue.
Introduction
Lactoferrin is part of the transferrin family of proteins. The protein is present in cow and human milk with a molecular mass of 80KDa. Lactoferrin is responsible for transferring irons to different types of cells in the body. It controls or regulates the irons that are present in the blood. pH as a factor can resist or inhibit the activities of other proteins, but lactoferrin can interact with iron at a certain pH range. Lactoferrin can bind to iron at 4.5 pH, but it cannot interact with iron to perform its function when pH is very low, for example, in the stomach of humans. It stops the regulation when the pH is about 2-3 in the stomach (i.e., the stomach becomes too acidic). The protein is also present in tears, white blood cells, seminal fluid, and saliva. It belongs to the innate immune system and helps fight viruses and bacteria that may enter the body of humans. Most biologists think of the human and bovine lactoferrin when they hear of lactoferrin. Bovine lactoferrin is highly mannose-containing with high N-glycan composition, while human lactoferrin is associated with low mannose and N-glycan composition when compared to bovine lactoferrin (Nwosu et al., 2012). Lactoferrin has a high binding affinity for iron (III) ions. Although it comes from the transferrin protein family, the iron-binding affinity of lactoferrin is higher than transferrin proteins.== Function ==
B
Disease
C
Irrelevance
D
Structural highlights
This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
