Digestion and Absorption Flashcards

1
Q

Define digestion

A

the breakdown of nutrients into absorbable molecules

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2
Q

Define absorption

A

the movement of nutrients, water and electrolytes from the gut lumen into the internal environment

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3
Q

Features of small intestine structure for absorption

A
  • surface of SI arranged in circular folds of Keckring
  • vill project from these folds
  • surface of villi covered in epithelial cells (enterocytes) with mucous secreting cells . Their apical surface covered by microvilli (brush border)
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4
Q

what does carbohydrate digestion begin with

A

salivary alpha-amylase

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5
Q

3 monosaccharides absorbed in the SI and transport

A

glucose (Na cotransporter SGLT1)
galactose (Na cotransporter SGLT1)
fructose (facilitated diffusion by GLUT5)

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6
Q

digestible vs indigestible glucose

A

1,4 alpha glycosidic bond (starch and glycogen)

plant cellulose 1,4 BETA glycosidic bond

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7
Q

two types of duodenal carbyhydrate enzymes AND what they do

A
pancreatic amylase (secreted from pancreas --> duodenum. digests internal alpha 1,4 glycosidic bonds. produces 3 things)
brush border enzymes (maltase, sucrase, lactase - act on disaccharides --> monosaccharides)
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8
Q

what three things does pancreatic amylase produce

what happens to them

A

WE ARE TRYING TO GET TO MALTOSE

maltotriose
maltose
alpha-limit dextrin

these are digested by oligosaccharides (alpha-glucosidase and isomaltase)

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9
Q

what does isomaltase do

A

cleaves alpha-1,6 glycosidic bonds in alpha-limit dextrin

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10
Q

what action does maltase, sucrase and lactase do

A

Maltase digest alpha 1,4 glycosidic bond

sucrase digests alpha 1,2 glycosidic bond

Lactase digests beta 1,4 glycosidic bond

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11
Q

what enzymes do we start and end with in protein digestion

A

stomach: pepsin
SI: pancreatic and brush border proteases

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12
Q

action of trypsinogen

A

use enterokinase in brush border to activate into trypsin

this is required to activate endopeptidases and exopeptidases

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13
Q

function of endopeptidases

A

cleave large polypeptides in middle of chain (oligopeptides)
eg. pepsin, trypsin, chymotrypsin, elastase

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14
Q

function of exopeptidases

A

clease amino acids one at a time from either end of protein
eg. carboxypeptidase
aminopeptidase

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