The Protein Buffer Systems

The protein buffers are very important in the plasma and the intracellular fluids but their concentration is very low in cerebrospinal fluid, lymph and interstitial fluids.

The proteins exist as anions serving as conjugate bases (Pr ⁻ ) at the blood pH 7.4 and form conjugate acids (HPr) accepting H⁺ .  They have the capacity to buffer some H₂CO₃  in the blood.

FACTORS AFFECTING ENZYME ACTIVITY

Velocity or rate of enzymatic reaction is assessed by the rate of change in concentration of substrate or product at a given time duration. Various factors which affect the activity of enzymes include:

1. Substrate concentration

2. Enzyme concentration

3. Product concentration

4. Temperature 5. Hydrogen ion concentration (pH)

6. Presence of activators

7. Presence of inhibitor

Effect of substrate Concentration :  Reaction velocity of an enzymatic process increases with constant enzyme concentration and increase in substrate concentration.

Effect of enzyme Concentration: As there is optimal substrate concentration, rate of an enzymatic reaction or velocity (V) is directly proportional to the enzyme concentration.

Effect of product concentration In case of a reversible reaction catalyzed by a enzyme, as per the law of mass action the rate of reaction is slowed down with equilibrium. So, rate of reaction is slowed, stopped or even reversed with increase in product concentration

Effect of temperature: Velocity of enzymatic reaction increases with temperature of the medium which they are most efficient and the same is termed as optimum temperature.

Effect of pH: Many enzymes are most efficient in the region of pH 6-7, which is the pH of the cell. Outside this range, enzyme activity drops off very rapidly. Reduction in efficiency caused by changes in the pH is due to changes in the degree of ionization of the substrate and enzyme.

Highly acidic or alkaline conditions bring about a denaturation and subsequent loss of enzymatic activity

Exceptions such as pepsin (with optimum pH 1-2), alkaline phosphatase (with optimum pH 9-10) and acid phosphatase (with optimum pH 4-5)

Presence of activators Presence of certain inorganic ions increases the activity of enzymes. The best examples are chloride ions activated salivary amylase and calcium activated lipases.

Effect of Inhibitors The catalytic enzymatic reaction may be inhibited by substances which prevent the formation of a normal enzyme-substrate complex. The level of inhibition then depends entirely upon the relative concentrations of the true substrate and the inhibitor

VITAMIN C: ASCORBIC ACID, ASCORBATE

Vitamin C benefits the body by holding cells together through collagen synthesis; collagen is a connective tissue that holds muscles, bones, and other tissues together. Vitamin C also aids in wound healing, bone and tooth formation, strengthening blood vessel walls, improving immune system function, increasing absorption and utilization of iron, and acting as an antioxidant.

RDA The Recommended Dietary Allowance (RDA) for Vitamin C is 90 mg/day for adult males and 75 mg/day for adult females

Vitamin C Deficiency

Severe vitamin C deficiency result in the disease known as scurvy, causing a loss of collagen strength throughout the body. Loss of collagen results in loose teeth, bleeding and swollen gums, and improper wound healing.

Anaerobic organisms lack a respiratory chain. They must reoxidize NADH produced in Glycolysis through some other reaction, because NAD⁺ is needed for the Glyceraldehyde-3-phosphate Dehydrogenase reaction (see above). Usually NADH is reoxidized as pyruvate is converted to a more reduced compound, that may be excreted.

The complete pathway, including Glycolysis and the re-oxidation of NADH, is called fermentation.

For example, Lactate Dehydrogenase catalyzes reduction of the keto group in pyruvate to a hydroxyl, yielding lactate, as NADH is oxidized to NAD⁺.

Skeletal muscles ferment glucose to lactate during exercise, when aerobic metabolism cannot keep up with energy needs. Lactate released to the blood may be taken up by other tissues, or by muscle after exercise, and converted via the reversible Lactate Dehydrogenase back to pyruvate

Fermentation Pathway, from glucose to lactate (omitting H⁺):

   glucose + 2 ADP + 2 P_i → 2 lactate + 2 ATP

Anaerobic catabolism of glucose yields only 2 “high energy” bonds of ATP.

Functions of  lipids

1. They are the concentrated fuel reserve of the body  (triacylglycerols).

2. Lipids are the constituents of membrane structure and regulate the membrane permeability (phospholipids  and cholesterol).

3. They serve as a source of fat soluble vitamins (A, D, E and K).

4. Lipids are important as cellular metabolic regulators (steroid  hormones and prostaglandins).

5. Lipids protect the internal organs, serve as insulating materials and give shape and smooth appearance to the body.

Cori Cycle

The Cori Cycle operates during exercise, when aerobic metabolism in muscle cannot keep up with energy needs.

For a brief burst of ATP utilization, muscle cells utilize ~P stored as phosphocreatine. For more extended exercise, ATP is mainly provided by Glycolysis.

Lactate, produced from pyruvate, passes via the blood to the liver where it is converted to glucose. The glucose may travel back to the muscle to fuel Glycolysis.

The Cori Cycle costs 6 P in liver for every 2P made available in muscle. The net cost is 4 P Although costly in terms of "high energy" bonds, the Cori Cycle allows the organism to accommodate to large fluctuations in energy needs of skeletal muscle between rest and exercise.