C because it's a good feeling but it can be stressful moving away from your family or whatever it is
Answer:
All blood types are made compatible with each other.
Explanation:
The different types of blood showed that not all blood types are compatible with each other. This is the reason why when a doctor transfer blood, this has to be compatible with the person's blood. Otherwise, the immune system will recognize the blood cells as antigens and proceed to destroy it.
Red blood cells in its surface can have different types of proteins, the proteins or lack of it that a person has determines the type of blood (A, B, AB). Also, if the cell has the Rh protein it will be positive, and if it does not have it, it will be negative. In total, we have eight blood types A+, A-,B+, B-,AB+, AB-,0+,0- and the compatibility depends on the proteins that a person has.
Answer:
Blue litmus paper turns red under acidic conditions and red litmus paper turns blue under basic or alkaline conditions, with the color change occurring over the pH range 4.5–8.3 at 25 °C (77 °F). Neutral litmus paper is purple. Litmus can also be prepared as an aqueous solution that functions similarly.
Explanation:
The structure of a typical antibody molecule
Antibodies are the secreted form of the B-cell receptor. An antibody is identical to the B-cell receptor of the cell that secretes it except for a small portion of the C-terminus of the heavy-chain constant region. In the case of the B-cell receptor the C-terminus is a hydrophobic membrane-anchoring sequence, and in the case of antibody it is a hydrophilic sequence that allows secretion. Since they are soluble, and secreted in large quantities, antibodies are easily obtainable and easily studied. For this reason, most of what we know about the B-cell receptor comes from the study of antibodies.
Antibody molecules are roughly Y-shaped molecules consisting of three equal-sized portions, loosely connected by a flexible tether. Three schematic representations of antibody structure, which has been determined by X-ray crystallography, are shown in Fig. 3.1. The aim of this part of the chapter is to explain how this structure is formed and how it allows antibody molecules to carry out their dual tasks—binding on the one hand to a wide variety of antigens, and on the other hand to a limited number of effector molecules and cells. As we will see, each of these tasks is carried out by separable parts of the molecule. The two arms of the Y end in regions that vary between different antibody molecules, the V regions. These are involved in antigen binding, whereas the stem of the Y, or the C region, is far less variable and is the part that interacts with effector cells and molecules.
