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Transcript
Digestion &Absorption of proteins Dietary Proteins • Through diet SOURCES Animal protein sources • Milk • Dairy byproducts • Meat • Egg • Fish • liver Plant Protein Sources • Cereals • Pulses • Peas • Beans • Nuts digestion In mouth • No protreolytic enzyme • Chewing • Mastication • Formation of bolus In stomach Gastric juice • Pepsin • Rennin • Gastriscin • Gelatinase Pepsin • Present in different species including mammals • Synthesized in stomach Cant act on • Keratins • Mucoproteins • Silk fibroins • Protamines can act on • Milk(casien) Rennin • Absent in adult humans • Also coagulates milk • Activity seen in babies Gastriscin • Gastric juice of humans • Requires acidic medium Gelatenase • Acts on gelatin • Requires an acidic medium Digestion in duodenum • Pancreatic juice present Some chief enzymes are • Trypsin • Chymotrypsin • Carboxypeptidase • collagenase Trypsin Hydrolyzes the • Arginine • Lysine Weak action on • Milk protein • Converts fibrinogen to fibrin • Can coagulate blood Chymotrypsin • Pancreatic juice of vertebrates • Hydrolyze milk protein(casien) Caboxypeptidase • Matalloenzyme • Specially Zink Collagenase • Acts on proteins present in collagen • yellow and white tissue fibers to yield peptides Digestion in small intestine • Enterokinase • Amino peptidase • Prolidase • Tri&di peptidase Enterokinase • Also known as enteropeptidase • Peptide bond connected to lysine Amino peptidase • Peptide to tripeptide • But not dipeptide Requires • Zn • Mg • Mn Prolidase • Terminal peptide bond connected to proline • Amino acid Tri&di peptidases • Hydrolyze peptides • In microvillus • A dipeptidase hydrolyzes a dipeptide • 2 molecules of amino acids • Requires Mn • Zn as co factor Absorption of amino acids • Ileum • Jejunum • Villi • Blood capillaries • Mysentry How do they reach liver • amino acids • Di peptidases • Tri peptidases • Carried by blood to liver Amino acid pool • All amino acids get mixed up in liver All tissues draw amino acids to synthesize • Tissue proteins • Enzymes • Protein hormones • To built cell structure Protein turn over • Protein constantly lost & resynthesized • Plasma proteins • Completely replaced every 15days • This state is also called continuing metabolism of amino acids Amino acids in blood • All amino acids occur in blood • Make total of 30-50mgS/100ml • Nitrogen is 4-5mg/100ml Circardian changes in plasma amino acid levels • Plasma level an amino acids does not remain constant throughout 24 hours • Lowest at 4am • Rise 15-35% by noon to early afternoon Tissue amino acids • Transported actively into tissues • Tissue uptake is favored by hormone • Insulin( growth hormone) • Testosterone( tissues) • Oestradiol( uterus) Liability of proteins • No special storage form • Always accomplished by tissue growth • During starvation liver proteins are used • Kidney and blood proteins come next Sources of blood amino acids • Dietary proteins (intestine) • Tissue breakdown • Synthesis in liver(exceot essential) Blood (30-50%amino acid pool) Utilization of amino acids • Tissue amino acids • Plasma protein formation • Formation of globin Hb • Enzyme protein • Protein hormones • Neurotransmitters • Proteins of milk • Glucose • Ketone body • Energy production • Urea formation Uses of amino acids • Protein synthesis • Variety of other components( Purine,pyrimidines etc) • Histamine • Biological fuel(10% energy production) Amino acid catabolism • Deamination • Removal of amino group • Catalyzed by transaminase enzyme • Product is alpha keto glutarate Whole metabolism • Dietary protein Amino acids • Body proteins • Other nitrogen containing compounds • Carbon skeletons • NH4 >UREA>EXCRETED • Acetyl coA • Pyruvate • ATP • GLUCOSE TYPESOF AMINO ACIDS • ESSENTIAL • NON ESSENTIAL ESSENTAIL AMINO ACIDS • • • • • • • • • Cant synthesize by organism Must be supplied by diet Arginine Histridine Isoleucine Leucine Lysine Methionine Phenyl alanine • Threonine • Tryptophan • valine Non essential amino acids • • • • • • • • Can be synthesized in the body Alanine Asparagine Aspartate Cysteine Glutamate Glycine Proline • Serine • Tyrosine Reference MEDICAL BIOCHMISTRY( 7th edition) BY:M N CHTTERJEW & RANA SHINDE THANKS
