2.8 & 2.9 Protein Digestion Flashcards

0
Q

Name the Non-Essential Ketogenic AA

A

NONE

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1
Q

Name the ketogenic Essential AA

A

Leucine and Lysine

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2
Q

Name the Glucogenic Essential AA

A

Histidine, THreonine, Methionine and Valine

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3
Q

Name the Glucogenic and Ketogenic Essential AA

A

Isoleucine
Tryptophan
Pheynlalanine

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4
Q

Name the Non essential Glucogenic and Ketogenic AA

A

Tyrosine

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5
Q

What is ketogenic?

A

An amino acid that is degraded to Acetyl-CoA or Oxaloacetate.
Cannot be converted to glucose

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6
Q

Role of HCl in protein digestion

A

Reduces pH to 1-2 which allows denaturation of dietary proteins

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7
Q

What activates Pepsin?

A

Low pH and other active autoactivate pepsin as well

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8
Q

Cholescystokinin is stimulated how in protein digestion and what are its function

A

It is stimulated by protein leaving the stomach
It stimulates release of pancreatic enzymes
It stimulates release of bile
It stimulates slow gastric empyting

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9
Q

Role of Secretin in Protein digestion

A

Activates release of bicarbonate solution from pancreas to neutralize the pH of intestine

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10
Q

What is the role of Enteropeptidase?

A

To convert trypsinogen to its active form trypsin

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11
Q

T or F, Pancreatic enzymes are released into small intestine as zymogens

A

True

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12
Q

What catalyzes Pepsinogen –> Pepsin

A

Low pH or other active pepsin

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13
Q

What is the role of pepsin

A

Degrade large peptide fragments and some free amino acids

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14
Q

What catalyzes Chymotrypsinogen –> CHymotrypsin

A

Tryspin

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15
Q

What substrates does chymotrypsin act on?

A

Aromatic Amino Acids

16
Q

What does Trypsin digest?

A

Arginine and Lysine residues

17
Q

Elastase has substrate specificity for what?

A

Hydrophobic Amino acids

18
Q

What are the major end products of protein digestion?

A

Free Amino Acids
Dipeptides
Tripeptides

19
Q

How are dipeptides and tripeptides transported across intestinal cell?

A

By using an H+ symporter

20
Q

How are Free Amino Acids transported into intestinal cell?

A

Using a Na Symporter

21
Q

How are all amino acids taken up by the capillary?

A

By using a Na Symporter

22
Q

What is Ubiquitin?

A

It is a marker that tags proteins for degradation by the proteasome

23
Q

T or F, Few Amino Acids are reincorporated into new proteins within the body

A

False, Most amino acids are.

24
Q

What are the three determinants of Protein longevity

A

Oxidation
PEST Sequences
Amino Terminal Residues

25
Q

What is the significance of Amino Terminal residues?

A

Some have high stabalizing residues while others have destabalizing. This determines the longevity of the AA

26
Q

What are the 4 PEST Sequences

A

Glutamate
Proline
Serine
Threonine