Answer:
Explanation:
A woman with type A blood (whose father was type O) meaning her genotype is AO mates with
Man that has type O blood (OO genotype)
Both are heterozygous for MN blood group and both also heterozygous for the FUT1 gene controlling the synthesis of the H substance (Hh)- which determines the expression of the A and B antigen.
Cross
A O M N H h
O AO OO M MM MN H HH Hh
O AO OO N MN NN h Hh hh
Type A- 1/2 O-1/2 type M- 1/4 MN-1/2 N- 1/4, type H- 3/4 h-1/4
Type A with M antigen:
1/2*1/4*3/4 = 3/32
Type A with M and N antigens:
1/2*1/2*3/4 = 3/16
Type A with N antigen:
1/2*1/4*3/4 = 3/32
Type O with M antigen:
1/2*1/4*3/4= 3/32
Type O with M and N antigens:
1/2*1/2*3/4 = 3/16
Type O with N antigen:
1/2*1/4*3/4 = 3/32.
The 3/4 value comes from the expression of Hh-3/4 (this determines if the A and B Angie will be expressed).
Answer:
D
Explanation:
Because don't have any p53 genes
Answer:
I think the answer is D. it would become plasma
Answer:
Disruption such as deforestation or mining can destroy the habitat, leading to water pollution, mud slides, and loss of soil. With the habitat affected, the animals the grey fox feeds on, such as rabbits or mice, will be affected as well, leading to the grey fox losing a source of food. By limiting the diet of the grey fox, other predators will be more likely to compete with the grey fox, disrupting its niche.
The answers are as follows:
1. <span>An inhibitor has a structure that is so similar to the substrate that it can bond to the enzyme just like the substrate: t</span>his is called competitive inhibitor. A competitive inhibitor will compete with the substrate for the active site of the enzyme and bind to the active site, thus incapacitating the substrate from binding to the active site.
2. An inhibitor binds to a site on the enzyme that is not the active site: this is called non competitive inhibitors. Non competitive inhibitors bind to other site in the enzyme which is not the active site of the enzyme. The binding of the inhibitor changes the conformation of the enzyme as well as the active site, thus making it impossible for the substrate to bind to the enzyme effectively.
3. <span>usually, a(n) inhibitor forms a covalent bond with an amino acid side group within the active site, which prevents the substrate from entering the active site or prevents catalytic activity: this is called irreversible or permanent inhibition. Permanent inhibitors form covalent bonds with the enzyme and prevent substrate from binding to the enzyme.
4. T</span><span>he competitive inhibitor competes with the substrate for the ACTIVE SITE on the enzyme: The active site of an enzyme is the place where the substrate normally bind in order to activate a enzyme. Competitive inhibitors are those inhibitors that compete with the substrate for the active site of the enzyme and prevent the substrate from binding there.
5. W</span><span>hen the noncompetitive inhibitor is bonded to the enzyme, the shape of the ENZYME is distorted. The non competitive inhibitors are those inhibitors that bind to other places in the enzyme instead of the active site. The binding of the non competitive inhibitor usually distort the shape and the conformation of the enzyme thus preventing the substrate from binding to it effectively.
6. E</span><span>nzyme inhibitors disrupt normal interactions between an enzyme and its SUBSTRATE. The principal function of enzyme inhibitor is to prevent the substrate from binding to the appropriate enzyme. This is usually done in the human system in order to regulate the activities of enzymes.</span>