B22 Digestion And Absorption Of Proteins Flashcards

1
Q

What kind of enzymes cleave internal peptide bonds

A

Endopeptidases

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

What enzymes cleave ends of protiens

A

Exopeptidases

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

What does HCl in the stomach do to proteins

A

Denature the,

Unfolding makes the protein more accessible to digest

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

What doe chief cells secrete

A

Pepsinogen

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

What si pepsinogen

A

Inactive precursor of pepsin

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

What can activated pepsin do

A

Auto catalyse the conversion of further mo,ecules of pepsinogen to pepsin

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

What does pepsinogen to pepsin stimulate the secretion of

A

Cck

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

What kind of protein structure is pepsinogen

A

Enzyme tertiary structure

Prosegment mask active site

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

What stimulates the secretion of sce retain

A

Acidity of stomach entering the duo

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

What kind of hormone is secretin

A

Peptide

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

What does secretin stillage

A

The secretion of bicarbonate rich pancreatic fluid to neutralise and dilute acid in duo

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

What does cck stimulate

A

Release of main digestive enzymes by the pancreas

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

What converts trypsinogen to trypsin

A

Duodenal enteropeptidases

Trios in can then auto activate

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

When trypsin is activated what can it do for the other zymogens

A

Activates them

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

How does the trypsin inhibitor inhibit trypsin

A

Lysine 15 in the inhibitor penetrates into the active site of enzyme and forms a salt bridge with aspartate in the active site

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

What are some pancreatic enzymes and their active forms

A

Chymotrypsinogen –> chymotrypsin
Trypsinogen –> trypsin
Pro elastase –> elastase
ProPhospholipase A2 –> phospholipase A2

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

Where is enteropeptidases produced and bound

A

Produced in the duodenum and bound to the brush border of the enterocytes

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

What does enteropeptidases do

A

Initaties the activation of pancreatic zymogens by activating trypsin which then activates other zymogens

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

Where does trypsin hydrolyse polypeptides on the chain

A

On the Carboxyl side of arginine and lysine residues

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

What does chymotrypsin bind

A

Aromatic amino acids as hydrophobic pocket

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

What does elastase interact with

A

Active site partially blocked by side chains of valine and threonine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
22
Q

What kind of amino acids can move via passive diffusion

A

Limited to hydrophobic amino acids such as tryptophan

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
23
Q

How most amino amino acid transport

A

Against conc grad which is via active mechanism

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
24
Q

Where are amino acid carrier systems

A

Exist in brush border of enterocyte basolateral border

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
25
How are di tri peptide transport into the enterocyte
By secondary active transport
26
How are the small si tri peptides transported across the brush border
By hydrogen ion dependant co porter
27
What do the basolateral facilitated diffusion not depend on
Sodium
28
What are some fat soluble vitamins
A K E D
29
What are some water soluble vitamins
B1- B9 | C
30
What is the chemical property of water and fat soluble vitamins
Water sol - hydrophilic | Fat sol - hydrophobic
31
How are water soluble vitamins excreted
In the urine
32
How are fat soluble,e vitamins excreted
Not stored in body
33
How are fat soluble vitamins carried
In Micelle and absorbed by the enterocytes
34
How are most water soluble vitamins absorbed
By simple passive diffusion
35
What are Cobalamins
4 metabolically imp forms of B12
36
What are Cobalamins released form their protein by
Pepsin and stomach acid
37
What are Cobalamins bound to
Glycoproteins haptocorrin which is sec by stomach
38
What does free Cobalamins bind to
Intrinsic factor
39
Heat does free B12 bind to
Trans cobalamin II
40
What does the B12 and trans cobalamin II do when in a complex
Leaves the cell Enters the portal vein Taken up by liver by receptor mediated endocytosis
41
How do u syn vit D3
Skin by Uv radiation of 7 - dehydrocholesterol
42
What happens to vitamin D3 after syn in skin
Carried in serum by vitamin binding protein | Hydroxyl acted in liver and then kidney
43
What si the final product of vit d3 syn
Calcitriol active form | 1,25-OH2D3
44
What does calcitriol do
Circulates the blood to control calciu metabolism and homeostasis in various tissue
45
What kind of hormone is calcitriol
Steroid hormone
46
What si vitamin D3 deficiency
Rickets | Osteomalacia
47
Where is calcium absorbed predominately
In the proximal small intestine
48
What are the two cellular calcium transport processes
Trans cellular abs stimulated by calcitriol | Para cellular
49
What are the steps for moving calcium across the enterocyte
Entry via one of 2 calcium channels Intracellular diffusion aided by transport molecule calbindin Extrusion from the cell mediated mainly by calcium ATPase on the basolateral border
50
The syn of calbindin and trpv6 are upregukated by
The active form of vit d
51
What is iron especially important for
Transfer of molecular oxygen present in Hb
52
What component does iron part of in Hb and myoglobin
Heme
53
Where else is iron found
Cytochrome a,b and c
54
What form is dietary iron
Ferric form Fe3+
55
Where is ferric form of iron reduced
In GI tract
56
What reduces the ferrous form of iron
Ascorbate and ferrireductase in brush border of enterocyte
57
How is fr2+ transported into the cells
By a divalent metak transporter
58
What happens to an excess of iron
Incomrp into a protien ferritin
59
How does iron be in crop into heme
Fe2+ ferrioxidase turns to Fe3+ which is then bound to transferrin in the plasma then take up by bone marrow rescued again and incorp to heme
60
What enzymes hydrolyse proteins
Peptidases