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phosphorus

  • All Known Essential Minerals

    Minerals (nutrients) are inorganic substances (contain no carbon) that are necessary for normal body function and development.

    Macrominerals

    Macro-minerals are needed in large doses (approximate recommended daily intake, milligrams (mg) per day ): 

    1. potassium, K (3500 mg) - metal, ions are necessary for the function of all living cells; 
    2. chloride, Cl− (3400 mg) - essential electrolyte in all body fluids; 
    3. sodium, Na, natrium (2400 mg) - metal, essential for all animals and some plants;
    4. calcium, Ca (1000 mg) - metal, essential for living organisms, produced in supernova nucleosynthesis;
    5. phosphorus, P (1000 mg) - in the form of the phosphate is required for all known forms of life; 
    6. choline (425 - 550 mg) - essential vitamin-like (vitamin B4) nutrient, synthesized in human body, but not sufficiently;
    7. magnesium, Mg (350 mg) - metal, essential for all known living organisms;

    Trace Minerals

    Trace minerals are needed in very small amounts (recommended daily intake, milligrams (mg) or micrograms (mcg) per day: 

    1. iron, Fe (15 mg) - metal, found in nearly all living organisms;
    2. zinc, Zn (8 - 11 mg) - metal, essential for humans and other organisms;
    3. manganese, Mn (5 mg) - metal, toxic essential trace element;
    4. fluorineF, fluoride ion, F− (3 - 4 mg) - a beneficial poisonous element, essential for bone solidity;
    5. copper, Cu (2 mg) - metal, essential to all living organisms;
    6. iodine, I (150 mcg) - a key component of thyroid hormones;
    7. selenium, Se (35mcg) - toxic in large doses, essential micronutrient for animals;
    8. chromium, Cr (30 mcg) - chromium (III) is questionably essential for humans.

  • Excessive Protein Intake

    Because the system for disposal of excess nitrogen is efficient, protein intakes moderately above requirement are believed to be safe.

    Brenner et al. (1982) postulated that excess protein intake accelerates the processes that lead to renal glomerular sclerosis, a common phenomenon of aging. There is supportive evidence from studies in animals, but not in humans on this point. Urinary calcium excretion increases with increased protein intake if phosphorus intake is constant. If phosphorus intake increases with protein intake, as it does in U.S. diets, the effect of protein is minimized.

    Habitual intakes of protein in the United States are substantially above the requirement, and although there is no firm evidence that these intake levels are harmful, it has been deemed prudent to maintain an upper bound of no more than twice the RDA for protein.

Plutarch

But for the sake of some little mouthful of flesh we deprive a soul of the sun and light, and of that proportion of life and time it had been born into the world to enjoy.

Protein Structure, Cooked and Denatured Proteins

Proteins are chains of amino acids. The sequence of amino acids in a chain is known as the primary structure of a protein. The chains fold up to form complex three dimensional shapes. The chains can fold on themselves locally (secondary structure) and wrap around themselves to form a specific three dimensional shape (tertiary structure).

The secondary / tertiary structure of a folded protein is directly related to its function. For example, enzymes are proteins that catalyze reactions. They have binding sites that interact with other molecules. These binding sites are created through the folding of the amino acid chains that gives rise to the three dimensional shape of the enzyme.

Denatured Protein

Denaturation of proteins involves the disruption and possible destruction of both the secondary and tertiary structures. Since denaturation reactions are not strong enough to break the peptide bonds, the primary structure (sequence of amino acids) remains the same after a denaturation process. Denaturation disrupts the normal sheets in a protein and uncoils it into a random shape.

Denaturation occurs because the bonding interactions responsible for the secondary structure (hydrogen bonds to amides) and tertiary structure are disrupted. In tertiary structure there are four types of bonding interactions between "side chains" including: hydrogen bonding, salt bridges, disulfide bonds, and non-polar hydrophobic interactions. which may be disrupted. 

Proteins can be denatured through exposure to heat or chemicals. Denatured proteins lose their three dimensional structure and thus their function. 

Digestion of Proteins and Cooking

Protein digestion begins in the stomach, where the acidic environment favors protein denaturation. Denatured proteins are more accessible as substrates for proteolysis than are native proteins. The primary proteolytic enzyme of the stomach is pepsin, a nonspecific protease that is maximally active at pH 2. Thus, pepsin can be active in the highly acidic environment of the stomach, even though other proteins undergo denaturation there.

Heat disrupts hydrogen bonds and non-polar hydrophobic interactions. This occurs because heat increases the kinetic energy and causes the molecules to vibrate so rapidly and violently that the bonds are disrupted

Foods are cooked to denature the proteins to make it easier for enzymes to digest them. Cooking food denatures some of the proteins in it and makes digestion more efficient. Heating to denature proteins in bacteria and thus destroy the bacteria.

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