Page 277 - Color Atlas of Biochemistry
P. 277
268 Tissues and organs
Digestive secretions Elastase mainly cleaves on the C side of the
aliphatic amino acids Gly, Ala, Val, and Ile.
Smaller peptides are attacked by carboxy-
A. Digestive juices
peptidases, which as exopeptidases cleave in-
Saliva. The salivary glands produce a slightly dividual amino acids from the C–terminal end
alkaline secretion which—in addition to water of thepeptides (seep. 176).
and salts—contains glycoproteins (mucins) as a–Amylase, the most important endoglyco-
lubricants, antibodies, and enzymes. sidase in the pancreas, catalyzes the hydroly-
D–Amylase attacks polysaccharides, and a li- sis of α1 4 bonds in the polymeric carbohy-
pase hydrolyzes a small proportion of the drates starch and glycogen. This releases mal-
neutral fats. α–Amylase and lysozyme, amu- tose, maltotriose, and a mixture of other oli-
rein-cleaving enzyme (see p. 40), probably gosaccharides.
serveto regulatethe oral bacterial flora rather Various pancreatic enzymes hydrolyze lip-
than for digestion (see p. 340). ids, including lipase with its auxiliary protein
Gastric juice. In the stomach, the chyme is colipase (see p. 270), phospholipase A 2 ,and
mixed with gastric juice. Due to its hydro- sterol esterase. Bile salts activate the lipid-
chloric acid content, this secretion of the gas- cleaving enzymes through micelle formation
tric mucosa is strongly acidic (pH 1–3; see (see below).
p. 270). It also contains mucus (mainly glyco- Several hydrolases—particularly ribo-
proteins known as mucins), which protects nuclease (RNAse) and deoxyribonuclease
the mucosa from the hydrochloric acid, salts, (DNAse)—break down the nucleic acids con-
and pepsinogen—the proenzyme (“zymogen”) tained in food.
of the aspartate proteinase pepsin (see Bile. The liver forms a thin secretion (bile)
pp. 176, 270). In addition, the gastric mucosa that is stored in the gallbladder after water
secretes what is known as “intrinsic factor”—a and salts have been extracted from it. From
glycoprotein needed for resorption of vitamin the gallbladder, it is released into the duode-
B 12 ( “extrinsic factor”) in the bowel. num. The most important constituents of bile
In the stomach, pepsin and related en- are water and inorganic salts, bile acids and
zymes initiate the enzymatic digestion of pro- bile salts (see p. 314), phospholipids, bile pig-
teins, which takes 1–3 hours. The acidic gas- ments, and cholesterol. Bile salts, together
tric contents are then released into the duo- with phospholipids, emulsify insoluble food
denum in batches, where they are neutralized lipids and activate the lipases. Without bile,
by alkaline pancreatic secretions and mixed fats would be inadequately cleaved, if at all,
with cystic bile. resulting in “fatty stool” (steatorrhea). Re-
Pancreatic secretions. In the acinar cells, sorption of fat-soluble vitamins would also
the pancreas forms a secretion that is alkaline be affected.
–
due to its HCO 3 content, the buffer capacity Small-intestinal secretions. The glands of
of which is suf cient to neutralize the stom- thesmall intestine(theLieberkühn and Brun-
ach’s hydrochloric acid. The pancreatic secre- ner glands) secrete additional digestive en-
tion also contains many enzymes that catalyze zymes into the bowel. Together with enzymes
the hydrolysis of high–molecular-weight food on the microvilli of the intestinal epithelium
components. All of these enzymes are hydro- (peptidases, glycosidases, etc.), these en-
lases with pH optimums in the neutral or zymes ensurealmostcompletehydrolysis of
weakly alkaline range. Many of them are the food components previously broken
formed and secreted as proenzymes and are down by the endoenzymes.
only activated in the bowel lumen (see
p. 270).
Trypsin, chymotrypsin, and elastase are en-
dopeptidases that belong to the group of ser-
ine proteinases (see p. 176). Trypsin hydro-
lyzesspecificpeptide bondson the Cside of
the basic amino acids Arg and Lys, while chy-
motrypsin prefers peptide bonds of the apolar
amino acids Tyr, Trp, Phe, and Leu (see p. 94).
Koolman, Color Atlas of Biochemistry, 2nd edition © 2005 Thieme
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