Real Property Concepts

Amino Acids: Main Role

• Primary function is the synthesis of structural and functional proteins.
• Body lacks a storage mechanism for proteins like it does for carbohydrates and fats.
• A 70kg person experiences about 400g of protein turnover daily, with equal amounts synthesized and broken down.

Essential vs Non-Essential Amino Acids

• Non-essential amino acids are sourced from diet or synthesized in the body.
• Essential amino acids solely obtained from the food we eat
• Deficiency in one essential amino acid stops protein synthesis.
• Essential amino acids give rise to non-essential ones, such as Glutamine.
• A deficit in any amino acids will result in a non formation of such protein
• Glutathione (Glu-Cys-Gly) transports amino acids into the cell
• Amino acid pool is constantly being created.
• Synthesis and degradation rates balance in adults, ensuring nitrogen equilibrium.

Protein Digestion: Initial Steps

• Dietary proteins denatured during cooking for easier digestion.
• Two classes of proteolytic enzymes are involved.
• Proteolytic enzymes are secreted in inactive zymogen forms and activated in the intestinal lumen to prevent autodigestion.

Proteolytic Enzymes: Types and Action

• Endopeptidases: Act on peptide bonds inside protein molecules, breaking them into smaller units.
  • Include Pepsinogen, Trypsinogen, Chymotrypsinogen, and Proelastase.
• Exopeptidases: Target peptide bonds at the ends of polypeptide chains.
  • Include Carboxypeptidase (acts on the carboxy-terminal end) and Aminopeptidase (acts on amino-terminal end).

Protein Digestion: Location

• Occurs in the stomach, pancreas and in intestinal cells

Gastric Protein Digestion

• Begins in the stomach with HCl secretion activates pepsinogen to pepsin.
  • HCl provides the correct pH for pepsin activity.
• Rennin (chymosin) present, active in infants only, aids in milk curdling

Milk Digestion in Infants

• Milk protein (Casein) converted to Paracasein by rennin.
• Resulting denatured protein (Part casein) then digested by pepsin.
• Pepsin is secreted by chief cells in the stomach as inactive pepsinogen.

Pepsin Activation & Function

• Pepsinogen converted to pepsin via removal of 44 amino acids from the N-terminal end with hydrochloric acid.
• Operates at optimum pH of around 2.
• Pepsin catalyzes hydrolysis of bonds formed by carboxyl groups of phenylalanine, tyrosine, tryptophan, and methionine.
• Breaks down proteins into proteases and peptones.

Pancreatic Protein Digestion

• Pancreatic enzymes function at an optimal pH of 8, provided by pancreatic juice and alkaline bile.
• Peptide hormones, cholecystokinin and pancreozymin stimulate pancreatic juice secretion.
• Pancreatic juice consists of endopeptidases: trypsinogen, chymotrypsinogen, proelastase, and procarboxypeptidase.
• Secreted in zymogen form to protect acinar cells.
• All are serine proteases, with serine residues at their active sites.

Trypsinogen Activation

• Activated by enteropeptidase (enterokinase) present on intestinal microvillus membranes.
• Once triggered, trypsin activates other enzymes molecules-chymotrypsinogen, proelastase, and procarboxypeptidase.
• Trypsin itself is activated by the removal of a hexapeptide from the N-terminal end.
• Catalyzes the hydrolysis of bonds formed by carboxyl groups of arginine and lysine.

Enzyme Specificity

• Chymotrypsin acts on aromatic amino acids, such as phenylalanine, tyrosine, tryptophan, valine, and leucine.
• Elastase acts on Glycine, Alanine and Serine (GAS)
• Premature activation of trypsinogen inside leads to autodigestion of the pancreas, resulting in acute pancreatitis.

Carboxypeptidases

• Trypsin and chymotrypsin degrade proteins into small peptides for further hydrolysis into dipeptides

Intestinal Protein Digestion

• Carboxypeptidases in the pancreatic juice aid digestion of tripeptides.
• These enzymes are metalloenzymes requiring zinc as a cofactor.
• It is brought abou by enzymes present in intestinal Juice
• Sulcus entericus aids completion of small peptides to amino acids

Intestinal Epithelial Enzymes

• Includes:
  • Leucine aminopeptidase: Release amino acids from N-terminal, basic amino acids and glycine.
  • Proline peptidase: Cleaves proline from polypeptides end
  • Dipeptidase & tripeptidase: Bring about protein digestion

Absorption of Amino Acids

• Occurs mainly in the small intestine via an energy-dependent process which requires a transport system
• These transport mediate processes and are ATP-dependent
• Five different transport systems exist for:
  • Neutral amino acids (alanine, valine, leucine, methionine, phenylalanine, tyrosine, isoleucine)
  • Basic Amino acids (lysine, agrinine and cysteine histidine)
  • Imino acids and Glycine
  • Acid A.A (Asp Glu)
  • Beta amino A.A

Meister Cycle (Gamma Glutamyl Cycle)

• In intestines, kidney and brain, the absorption of neutral amino acids depends on the gamma glutamyl cycle.
• Central role played by tripeptide glutathione (GSH): gamma-glutamyl-cysteinyl-glycine.
• Reacts with amino acid to create gamma-glutamyl amino acid.
• Catalyzed by gamma-glutamyl transferase.
• Gamma-glutamyl amino acid is cleaved forming amino acid, a process that requires ATP.
  • The net amino acid is created across membrane

Interorgan Amino Acid Transport

• Breakdown of muscle protein offers amino acid source for tissues
• Tiver site disposal Plasma acid are seen in low concentrations, excluding glutamic acid and glutamine
• Glutamine seen in higher concentrations Muscle releases alanine and glutamine mainly Livers reoves amino group converted to urea and carbon skeleton in gluconeogensis Branched chained amino acid is taken to provide brain energy

Amino Acid Absorption: Fed State

• Tissues take in Amino acids from the diet differently
• Brain & Muscle take in amino acids with branched chains and release alanine and glutamine.
• Gllutamine releases to kidneys and alanine helps regulate acid-base balance

Formation of Ammonia

• Remove of an amino acids for interorgan transport
• Breakdown is the main amino source in the body
• Small ammonias may be form from purines
• Its toxic. Thus urea ex created through unine
• All amino transferred Also N5: The exchange of the alpha is called interconversion

Transamination

• Transfered for amino acid produce Skeleton of ketoacrd
• Ammo group is ecreted white the ketoacrd

Meister Cycle

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• The process used for protein synthesix
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This quiz assesses understanding of real property concepts. Topics covered include leases vs. licenses, life estates, concurrent ownership, and easements. Test your knowledge of property law.