Digestion & Absorption Flashcards

1
Q

What is protein metabolism ?

A

Various biochemical processes involved in the synthesis of protein and amino acids and in the breakdown of proteins by catabolism.
I.e. can be anabolic or catabolic

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2
Q

Organic monomeric units from which proteins are synthesized are called

A

Amino acids

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3
Q

What is the basic function of protein?

A

It acts as an enzyme in and around the cell

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4
Q

Which animal source of protein is not considered to be high class protein ?

A

Gelatin

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5
Q

Peptidases (proteolytic enzymes) are divided into what and what ? Explain each.

A

Endopeptidases - hydrolyze the peptide bonds in the main polypeptide structure, breaking it down to amino acids e.g pepsin, trypsin, chymotrypsin.

Exopeptidases - hydrolyse the peptide bonds adjacent to the amino and carboxyl terminal residues. E.g carboxypeptidases, aminopeptidases.

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6
Q

Protein digestion is divided into ?

A

Gastric
Pancreatic
Intestinal

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7
Q

Protein Digestion begins chemically where?

A

The stomach

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8
Q

Explain the gastric digestion of proteins

A

.Gastric juice secreted in stomach contains HCL and Pepsinogen
. HCL kills bacteria that may denature protein
. Pepsinogen is secreted as an inactive ZYMOGEN (has extra amino acids to prevent self destruction)
. It is activated by HCL or by the auto catalytic activity of already activated pepsin.
. Pepsin is an endopeptidase and hydrolyses peptide bonds to polypeptide chains and a few free amino acids

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9
Q

What are the polypeptide hormones secreted when polypeptides enter the duodenum ?

A

CHOLECYSTOKININ and SECRETIN

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10
Q

What are the 4 enzymes (inactive form) secreted by the pancreas for protein digestion.

A
  1. Trypsinogen
  2. Chymotrypsinogen
  3. Procarboxypeptidases A&B
  4. Proelastases
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11
Q

What enzyme causes the activation of trypsin?

A

Enterokinase

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12
Q

Explain the specificity of the active pancreatic proteolytic enzymes

A

TRYPSIN - hydrolyses peptide bonds of basic amino acids (Lys and Arg)
CHYMOTRYPSIN - hydrolyses peptide bonds of aromatic acids linking the amino group of another amino acid other than glutamate and aspartate
ELASTASE - hydrolyses peptide bonds adjacent to small neutral amino acids residues
CARBOXYPEPTIDASE- further degrades peptides into free amino acids and dipeptides.

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13
Q

What are the two sources of proteins?

A

1) dietary proteins - 70-150g
2) endogenous proteins - 35 - 200g (as a result of protein synthesis)

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14
Q

Enzymes involved in the hydrolysis of proteins are called

A

Peptidases

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15
Q

Nutritional value or quality of a protein is determined by a combination of two factors

A

1) protein digestibility
2) essential amino acid content

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16
Q

Infant stomachs produce an additional enzyme called __ which prevents the quick removal of milk from the stomach

A

Rennin or chymosin

17
Q

__ regulates the activity of intestinal proteolytic enzymes

A

Pancreatic trypsin inhibitor

18
Q

Carboxypeptidase A attacks _

A

Carboxyl terminal peptide linkages of polypeptides

19
Q

Carboxypeptidase B acts on __

A

It acts on peptide linkages adjacent to amino or basic amino acid residues

20
Q

What are the major enzymes of the mucosal secretions of the glands of Brunner and Lieberkuhn (in the intestine)

A

Aminopeptidases and dipeptidases

21
Q

Aminopeptidases are ___

A

1) non-specific for amino acids
2) do not hydrolyze didpeptides
3) are Mg2+ and Mn+
4) hydrolyze successive amino terminal residues for short peptides but not when there is a free carboxyl terminal in the area.

22
Q

Dipeptidases are __

A

1) specific for amino acids
2) complete digestion of dipeptides to free amino acids

23
Q

Prolinases ____

A

Hydrolyze peptides or dipeptides containing PROLINE or Hydroxyproline as N-terminals