Chp. 35

Question 1

This protease is released in the stomach and cleaves proteins at aromatic and acidic amino acid side chains?

Answer 1

Pepsin

via pepsinogen

Question 2

This protease is released by the intestinal brush border cells and is key to activating the subsequent pancreatic proteases?

Answer 2

Enteropeptidase

AKA “Enterokinase”

Question 3

Secreted as a zymogen by the pancreas this protease is the first activated by enteropeptidase and shows specificity for basic amino acid side chains.

Answer 3

Trypsin

Via trypsinogen

Question 4

Secreted as a zymogen by the pancreas this protease is activated by trypsin and shows specificity for aromatic amino acid side chains.

Answer 4

Chymotrypsin

Question 5

Pancreatic protease which attacks the carboxy- end of peptides releasing one amino acid at a time. The “A” version prefers this class of amino acids?

Answer 5

Hydrophobic Amino Acids

Question 6

Family of protease which trypsin, chymotrypsin and elastase belong to based on active site homology?

Answer 6

Serine proteases

Question 7

These lysosomal proteases are “cysteine” proteases which cleave after aspartate.

Answer 7

Clathepsins

and Caspases

Question 8

Large cytoplasmic complex which breakdown ubiquinated cellular proteins?

Answer 8

The proteasome

Question 9

The PA700 cap complex activates a proteasome to become specific for these proteins?

Answer 9

Ubiquinylated proteins

Question 10

The PA28 cap complex activates a proteasome to become specific for these proteins?

Answer 10

Short peptides

Question 11

The majority of amino acids are transported across the intestinal membranes by co-transport with this ion?

Answer 11

Na+

Question 12

Location of most active amino acid transport mechanisms for dietary amino acids?

Answer 12

The intestinal “brush border”

Question 13

This organ filters out nitrogenous wastes and most simple amino acids. It reclaims the amino acids using secondary active transport.

Answer 13

The kidneys

Question 14

Amino acids of this type are transported across the membranes of tissues independently of Na+

Answer 14

Branched chain and aromatic amino acids

Question 15

Name the 3 non-polar, branched chain amino acids

Answer 15

Valine, leucine and isoleucine

Question 16

This protein has a high turnover due to the short half-life of the cells which contain it?

Answer 16

Hemoglobin

Question 17

Muscle proteins (especially alanine) are turned over to carry out this liver biosynthetic pathway?

Answer 17

Gluconeogenesis

Question 18

As intestinal epithelial cells are sloughed off, these proteins are lost and hence have a high turnover rate.

Answer 18

Digestive enzymes

Question 19

This amino acid is used to cycle amino groups to the liver while returning glucose to muscle?

Answer 19

Alanine

Question 20

Since proteins cannot be used for energy storage, name 2 forms of macromolecules which the carbons from amino acids can be converted for storage?

Answer 20

Glycogen

Triglycerides

Question 21

These cellular structures consist of cytoplasmic components are surrounded by membranes?

Answer 21

Autophagolysosomes

Question 22

Lysosomal proteases that degrade proteins to amino acids and are triggered by starvation?

Answer 22

Clathepsins

Question 23

Insulin causes Akt to phosphorylate this protein at a different site, inactivating it

Answer 23

TSC1/TSC2

Question 24

This 76 aa protein covalently binds to e-amino group of lys in proteins; Marking them for degradation by Proteasomes

Answer 24

Ubiquitin

Question 25

This regulatory subunit requires ATP to unfold & push proteins through cylinder of the proteasome?

Answer 25

The 19S subunit

The regulatory particle

Question 26

This enzyme found in the cell membrane can transfer an amino acid onto glutathione. Then, once on inside of membrane, Cysteinylglycine & Glutamyl-amino acid are released

Answer 26

g-Glutamyl Transpeptidase