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DIETARY PROTEINS SERVE 3FUNCTIONS
1. THEIR CONSTITUTENT AMINOACIDS ARE USED FOR SYNTHESIS OF BODY PROTEINS
2. THE CARBON SKELETONS OF THE AMINO ACIDS ARE OXIDISED TO YIELD ENERGY
3. THEIR CARBON & NITROGEN ATOMS MAY BE USED TO SYNTHESISE OTHER ‘N’ CONTAINING CELLULAR CONSTITUENTS AS WELL AS MANY NON-NITROGEN CONTAINING METABOLITES
1.DIGESTION IN STOMACH
ENTERING PROTEINS (+) GASTRIN (+) GASTRIC JUICE (pH 1.5 – 2.5) CONTAINING
1. HCL2. PEPSINOGEN3. RENNIN (IN INFANTS)
HYDROCHLORIC ACID
• SECRETED BY PARIETAL CELLS• KILLS MICRO-ORGANISMS• DENATURES PROTEIN MAKING
INTERNAL PEPTIDE BONDS MORE SUSCEPTIBLE TO SUBSSEQUENT HYDROLYSIS BY PROTEOSES
• PROVIDES ACID ENVIRONMENT FOR PEPSIN ACTION
PEPSIN
• SECRETED BY CHIEF CELLS AS PEPSINOGEN – INACTIVE PRECURSOR
• CONVERTED TO ACTIVE PEPSIN BY AUTOCATALYSIS
• WORKS AT ACIDIC pH• CLEAVES PEPTIDE BONDS
INVOLVING AROMATIC & ACIDIC AA
RENNIN
• CHYMOSIN / RENNET• IMPORTANT IN INFANTS DIGESTIVE
PROCESS• CLOTTING OF MILK
R Ca++
CASEIN PARACASEIN Ca++PARACASEINATE
THE PURPOSE OF THIS REACTION IS TO CONVERT MILK INTO MORE SOLID FORM TO PREVENT THE RAPID PASSAGE OF MILK FROM STOMACH OF INFANTS
2.DIGESTION IN INTESTINEBY PANCREATIC ENZYMES
ACIDIC CONTENTS (CHYME) PASSING INTO SMALL INTESTINE TRIGGERS THE SECRETION OF
1. SECRETIN 2. CHOLECYSTOKININ
SECRETIN
• STIMULATES PANCREAS TO SECRETE BICARBONATE & RELEASE OF PANCREATIC JUICE INTO THE SMALL INTESTINE.
• NEUTRALISES GASTRIC HCL CHANGING pH FROM 1.5 – 7.0
CHOLECYSTOKININ
• STIMULATES SECRETION OF PANCREATIC ENDOPEPTIDASE & EXOPEPTIDASE
• ENDOPEPTIDASE INCLUDES CHYMOTRYPSIN & ELASTASE, CLEAVING INTERNAL PEPTIDE BONDS
• EXOPEPTIDASE CLEAVES 1 AA AT A TIME FROM EITHER ‘C’ OR ‘N’ END. INCLUDES CARBOXYPEPTIDASE & AMINOPEPTIDASE
ACTIVATION OF PANCREATIC PRO-ENZYMES
TRYPSINOGENENTEROPEPTIDASE
TRYPSINCHYMOTRYPSINOGEN CHYMOTRYPSIN
PRO-ELASTASE ELASTASE
PROCARBOXYPEPTIDASE CARBOXYPEPTIDASE
• TRYPSIN – HYDROLYSES PEPTIDE BONDS WHOSE CRBOXYL GROUPS ARE CONTRIBUTED NY LYS & ARG RESIDUES
• CHYMOTRYPSIN-CLEAVES PEPTIDE BONDS INVOLING CARBOXYL GROUP OF AROMATIC AA
• ELASTASE – HYDROLYSES THOSE PEPTIDE BONDS FORMED BY SMALL NON-POLAR AA RESIDUES SUCH AS ALA, SER & GLY
• THUS 3 ENZYMES HYDROLYSE POLYPEPTIDES TO SMALLER PEPTIDES
Degradation of short peptides in the small intestine is continued by an EXOPEPETIDASE- CARBOXYPEPTIDASEwhich removes the successive carboxy terminal aa residues from peptide
1. CARBOXYPEPTIDASE ‘A’ – RELEASES HYDROPHOBIC AA
2. CARBOXYPEPTIDASE ‘B’ – RELEASES BASIC AA
3.DIGESTION IN INTESTINEBY INTESTINAL PROTEOSES
• The digestion is completed by the PEPTIDASES of the mucosa of the small intestine namely:
1. AMINOPEPTIDASES2. GROUP OF DIPEPTIDASES
AMINO-PEPTIDASE- EXOPEPTIDASE- REQUIRE Mg/Mn - HYDROLYSE PEPTIDE BONDS
NEXT TO N-TERMINAL AA OF SHORT PEPTIDES
DIPEPTIDASES- COMPLETE THE DIGESTION OF
DIPEPTIDES TO FREE AMINO ACIDS
ABSORPTION OF AMINOACIDS
• MOSTLY THRU ACTIVE TRANSPORT
• 5 SEPARATE SYSTEMS – TRANSPORT L-AMINOACIDS FROM INTESTINAL LUMEN INTO INTESTINAL EPITHELIAL CELLS
• THUS AA RELEASED BY DIGESTION PASS FRM GUT THRU HEPATIC PORTAL VEIN TO THE LIVER
• TRANSPORT SYSTEM ALSO PRESENT IN RENAL SYSTEM
TRANSPORT SYSTEM
AMINOACID TRANSPORTD
DISORDER
Small neutral aminoacids
Ala Ser & Thr HARTNUP Disease
Large neutral aminoacids
Isoleu, Leu, Val,Tyr,Trp,Phe
Basic aa & Cysteine
Arg, Lys, Ornithine, Cys
CYSTINUTIA
Acidic aminoacids
Glutamic acid Aspartic acid
Iminoacid, Glycine
Pro, Hydroxy pro, Gly
GLYCINURIA