NEET MDS Lessons
Biochemistry
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
Factors regulating blood calcium level
(i) Vitamin D
(a) Vitamin D and absorption of calcium: Active form of calcium is calcitriol. Calcitriol enters intestinal wall and binds to cytoplasmic receptor and then binds with DNA causes depression and consequent transcription of gene code for calbindin. Due to increased availability of calbindin, absorption of calcium increases leading to increased blood calcium level.
(b) Vitamin D and Bone: Vitamin D activates osteoblast, bone forming cells & also stimulates secretion of alkaline phosphatase. Due to this enzyme, calcium and phosphorus increase.
(c) Vitamin D and Kidney: Calcitriol increase reabsorption of calcium and phosphorus by renal tubules.
(ii) Parathyroid hormone (PTH)
Normal PTH level in serum is 10-60ng/l.
(a) PTH and bones: In bone, PTH causes demineralization. It also causes recreation of collagenase from osteoclast leads to loss of matrix and bone resorption. As a result, mucopolysacharides and hydroxyproline are excreted in urine.
(b) PTH and Kidney: In kidney, PTH causes increased reabsorption of calcium but decreases reabsorption of phosphorus from kidney tubules.
(iii) Calcitonin Calcitonin decreases serum calcium level. It inhibits resorption of bone. It decreases the activity of osteoclasts and increases osteoblasts.
Hyper Calcemia When plasma Ca2+ level is more than 11mg/dl is called Hypercalcemia. It is due to parathyroid adenoma or ectopic PTH secreting tumor. calcium excreted in urine decreases excretion of chloride causing hyperchloremic acidosis.
Hypocalcemia Plasma calcium level less than 8mg/dl is called hypocalcemia. Tetany due to accidental surgical removal of parathyroid glands or by autoimmune disease. In tetany, neuromuscular irritability is increased. Increased Q-7 internal in ECG is seen. Main manifestation is carpopedal spasm. Laryngismus and stridor are also observed.
ZINC
The enzyme RNA polymerase, which is required for transcription, contains zinc and it is essential for protein bio synthesis.
Deficiency in Zinc leads to poor wound healing, lesions of skin impaired spermatogenesis, hyperkeratosis, dermatitis and alopecia
Clinical significance
Primary hyperparathyroidism is due to autonomous, abnormal hypersecretion of PTH in the parathyroid gland
Secondary hyperparathyroidism is an appropriately high PTH level seen as a physiological response to hypocalcemia.
A low level of PTH in the blood is known as hypoparathyroidism and is most commonly due to damage to or removal of parathyroid glands during thyroid surgery.
The Phosphate Buffer System
This system, which acts in the cytoplasm of all cells, consists of H2PO4– as proton donor and HPO4 2– as proton acceptor :
H2PO4– = H+ + H2PO4–
The phosphate buffer system works exactly like the acetate buffer system, except for the pH range in which it functions. The phosphate buffer system is maximally effective at a pH close to its pKa of 6.86 and thus tends to resist pH changes in the range between 6.4 and 7.4. It is, therefore, effective in providing buffering power in intracellular fluids.
SELENIUM
normal serum level is 50-100 mg/day
Selenium dependent enzymes include glutathione Peroxidase and 5-de-iodinase. Selenium concentration in testis is the highest in adult. It is very necessary for normal development and maturation of sperm.
3-D Structure of proteins
Proteins are the main players in the life of a cell. Each protein is a unique sequence of amino acid residues, each of which folds into a unique, stable, three dimentional structure that is biologically functional.
Conformation = spatial arrangement of atoms that depends on rotation of bonds. Can change without breaking covalent bonds.
- Since each residue has a number of possible conformations, and there are many residues in a protein, the number of possible conformations for a protein is enormous.
Native conformation = single, stable shape a protein assumes under physiological conditions.
- In native conformation, rotation around covalent bonds in polypeptide is constrained by a number of factors ( H-bonding, weak interactions, steric interference)
- Biological function of proteins depends completely on its conformation. In biology, shape is everything.
- Proteins can be classified as globular or fibrous.
There are 4 levels of protein structure
- Primary structure
- linear sequence of amino acids
- held by covalent forces
- primary structure determines all oversall shape of folded polypeptides (i.e primary structure determines secondary , tertiary, and quaternary structures)
- Secondary structure
- regions of regularly repeating conformations of the peptide chain (α helices, β sheets)
- maintained by H-bonds between amide hydrogens and carbonyl oxygens of peptide backbone.
- Tertiary structure
- completely folded and compacted polypeptide chain.
- stabilized by interactions of sidechains of non-neighboring amino acid residues (fibrous proteins lack tertiary structure)
- Quaternary structure
- association of two or more polypeptide chains into a multisubunit protein.