Quote:
Originally Posted by The Manager
The way that food is cooked is absolutely essential for avoiding unnecessary nutrient loss. The longer a food is exposed to heat, the greater the nutrient loss. Being submersed in hot water (boiling) creates more nutrient loss than steaming (surrounding with steam rather than water) if all other factors are equal.
|
The above quoted part is the answer of my last question but insufficient one. Here is the detail...
The vitamin loss due to the exposure of the vitamins to heat is most particular to Vitamin C and Vitamin E which are sensitive to oxidation, especially when heated in contact with metals or alkali.
There are two categories of vitamins based on their solubility. The first set is the soluble vitamins which include Vitamin B Complex and Vitamin C. Other set is the fat (or lipid) soluble Vitamins which include Vitamin A, D, E and K. So vitamin loss due to boiling is most particular to B complex group which you have mentioned above.
As I have just read before logging in on the forum,
the vitamin loss is usually due to their storage; i e vitamins cannot be kept for a longer period of time. That is the reason why we read on many supplement bottles "
Extra/Excess vitamins have been added to make up the loss that occurs due to their storage".
Let's understand how vitamin loss can actually take place.
I'm going to detail you about same as follows:
Vitamin A: It is sensitive to oxygen and light. It means that too much of oxygen and light is essentially going to result in the loss of Vitamin A.
Vitamin D: There is usually very little loss of this vitamin. It is synthesized by ultraviolet radiations that we get from the sun. It is synthesized within the body itself. Humans don't have to this vitamin much.
Vitamin K: It is sensitive to acids, alkali, light and oxidizing agents.
Riboflavin: It is additionally sensitive to light. The loss of riboflavin can be caused due to boiling also as it is a water soluble vitamin ( i e it is a vitamin of B Complex group).
The rest of the detail shared in the same post is worthwhile too brother.
Quote:
Originally Posted by The Manager
Hemoglobin/Oxygen Binding
The primary function of hemoglobin (Hb) is to transport oxygen. Since oxygen is not very soluble in water (the major constituent of blood), an oxygen transport protein must be used to allow oxygen to be 'soluble'. Hemoglobin (Hb) is the oxygen transport protein used in the blood of vertebrates. Below is a wireframe diagram of a hemoglobin molecule. It is composed of 4 polypeptide chains (represented in this diagram by different colors. Each chain contains one heme group (colored orange), each of which contains one iron ion (not shown). The iron is the site of oxygen binding; each iron can bind one O2 molecule thus each hemoglobin molecule is capable of binding a total to four (4) O2 molecules.
|
The above quoted part is the detailed answer of my question number three. So the co-factor or co-enzyme that assists hemoglobin in the oxygen-transport within the blood is
HEME. It is the heme that binds oxygen with hemoglobin or takes up oxygen and releases it at right places. It also takes up Carbon Dioxide and releases it. In the above quoted bit of your post the answer of the question number four could have been given which I have just had a little earlier. The amount of oxygen present in a sample of arterial blood in a healthy human which is chemically combined with hemoglobin is about 98.5%. The other 1.5% is dissolved in the other blood liquids and not connected to the hemoglobin.
The other details given in the same post are a precious to my knowledge.
Quote:
Originally Posted by The Manager
In mammals, the protein makes up about 97% of the red blood cells' dry content, and around 35% of the total content (including water).
|
The above quoted part is the answer of Q2. Thanks for putting other relevant details.
Note: There is still one question that remains unanswered and that is the Q1.
Why co-factors are required by certain enzymes to carry out their biological activity whereas many enzymes like protease, carbohydrates, lipase etc can carry out metabolic activities without any assistance?
I've just got the answer to this question on internet a little while earlier.
Let us understand it here.
As we know that most enzymes are proteins (or nucleic acids). Some chemistry is not possible with amino acids/ nucleotide functional groups.
The reason why the chemistry is not possible is because certain amino acids are limited in their backbone structure ( i e limited in the number of r-group ).
Since it is not possible for all amino acids to chemically combine with certain enzymes, the enzymes therefore require co-factors or con-enzymes to loosely or tightly bind to them and thus assist in carrying out the perfect protein or enzyme activity.
Thanks for providing me such a great deal of information on the questions asked above. I will keep adding the relevant facts to this thread as I study further...
Regards