<u>Answer:</u>
<em>The steps in making packaging and exporting a protein from a cell are listed below in the following points:</em>
- <em>Protein is made from the Ribosomes.</em>
- <em>These proteins are gathered in the endoplasmic reticulum. </em>
- <em>From ER the proteins are exported to the Golgi bodies. These Golgi apparatus is found in the vesicles.</em>
- <em>The Golgi bodies modify the protein to suitable forms that can be absorbed.</em>
- <em>Finally it is transported to all part of cells in our body.</em>
Answer is: coupled transport differs from primary active transport due to the fact that it uses electrochemical potential difference as a direct source of energy.
Primary active transport directly uses metabolic energy (adenosine triphosphate- ATP) to transport molecules across a membrane.
In secondary active transport (coupled transport) there is no direct coupling of ATP, <span>energy derived from the pumping of protons across a cell membrane.</span>
Answer:
Al introducir una piedra en agua, está se va al fondo del vaso, por que es más pesada que el agua
Al introducir un bolígrafo, este flota, por que es más liviano que el agua
Si se introduce en agua un tajalapiz se evidenciará un proceso de corrosión del metal
Debido a la reacción con el agua, sin embargo el efecto será más evidente si se agrega sal a la mezcla
Answer:
The right answer for the blank is cleavage.
Explanation:
After fertilization the next step is cleavage in which zygote divide mitotically. As the embryo move from oviduct down the fallopian tube it divide into two cell and then four cells. four cell embryo is known as blastomere.
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>
