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Biochem Final > Section 1 > Flashcards

Section 1 Flashcards

1
Q

pH of arterial plasma

A

7.35-7.45

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2
Q

pH of extracellular fluid

A

6.8-7.8

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3
Q

pH within cells

A

6.9-7.4

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4
Q

If pH<pKa, then what form predominates?

A

acid

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5
Q

If pH>pKa, then what form predominates?

A

basic

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6
Q

what is the buffer system of blood?

A

bicarbonate

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7
Q

What is the intracellular buffer system?

A

phosphate

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8
Q

What is this condition?

increase in partial pressure of CO2

A

resipratory acidosis

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9
Q

What is this condition?

decrease in partial pressure of CO2

A

respiratory alkalosis

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10
Q

What is this condition?

decrease in HCO3- concentration

A

metabolic acidosis

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11
Q

What is this condition?

increase in HCO3- concentration

A

metabolic alkalosis

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12
Q

What condition is due to decrease in lung function and how will the body do to compensate?

A

Respiratory Acidosis

  • kidneys will try to compensate by increasing bicarbonate
  • all compensatory reaction by the kidneys will take several days
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13
Q

What condition is due to hyperventilation and what will the body do to compensate?

A

Respiratory Alkalosis

- kidneys will try to compensate by excreting bicarbonate in urine

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14
Q

What condition can be caused by decreased kidney function or body trying to compensate for an already existing acidosis, such as DKA? How will the body try to compensate?

A

Metabolic Acidosis

  • lungs will attempt to compensate by “blowing off” CO2
  • this effect will take place within minutes and complete within 12 - 24 hours
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15
Q

What condition can be caused by an excess administration of bicarbonate or loss of H+ (from prolonged vomiting or use of diurectics)? How will the body compensate?

A

Metabolic Alkalosis

- lungs will attempt to compensate by breathing less (hypoventilation), trying to keep as much CO2 as possible

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16
Q

What type of protein structure is this?

structure results from hydrogen bonding interactions between C=O and H-N of the backbone

A

Secondary structure

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17
Q

What type of protein structure is this?

subunits associate with each other through non-covalent interactions?

A

quaternary

18
Q

What type of protein structure is this?
sequence of amino acid residues in a polypeptide chaing
- determines 3-D structure and biological function of the protein

A

primary

19
Q

What type of protein structure is this?
non-covalent interactions are the major element in formation of this structure (H-bonding, hydrophobic forces and van der Waal’s)

A

tertiary

20
Q

What type of enzyme is this?

catalyzes cleavage of bonds with water

A

hydrolases

Ex. glucosidases, ATPases

21
Q

What type of enzyme is this?

catalyzes redox reactions, transfer of electrons

A

oxidoreductase

Ex. NAD+»NADH

22
Q

What type of enzyme is this?

catalyzes transfer of functional groups

A

transferases

Ex. kinases, aminotransferases

23
Q

What type of enzyme is this?

catalyzes formation of bonds between carbons and other atoms

A

ligases

Ex. synthase, synthetase, carboxylase

24
Q

What type of enzyme is this?

cleaves bonds without water

A

lyases

Ex. aldose B

25
Q

What type of enzyme is this?

changes stereochemistry

A

isomerase

26
Q

Holoenzyme

A

apoenzyme with prosthetic group

- active

27
Q

Apoenzyme

A

apoenzyme without its prosthetic group

- inactive

28
Q

Vmax, conditions

A

more substrate will not increase reaction rate, but more enzymes will
- does not depend of concentration of subtrate

29
Q

Km, conditions

A
  • more enzymes will not change this value
30
Q

What does a low Km mean?

A

increase substrate affinity
- takes more substrate to be at Vmax/2
this explains why glucokinase can turn over more G6P from glucose than hexokinase

31
Q

What does a high Km mean?

A

decrease substrate affinity

- takes only small amount of substrate to be at Vmax/2

32
Q

Conditions of competitive inhibition

A 
Vmax - no change because it's independent of substrate concentration
Km increases (substrate concentration dependent)
- less substrates are binding
33
Q

Conditions of non-competitive inhibition

A 
Vmax decreases (number of enzymes changed due to the inhibition)
Km - no change
- fewer working enzymes
34
Q

Gs G-proteins

A

stimulates adenylate cyclase to form cAMP

35
Q

Gi G-proteins

A

inhibits adenylate cyclase

36
Q

Gq G-proteins

A

stimulates phospholipase C to form IP3/DAG

37
Q

Which is better at binding to oxygen during low levels of O2, myoglobin or hemoglobin?

A

myoglobin

38
Q

What is better at binding to oxygen during high levels of O2, myoglobin or hemoglobin?

A

hemoglobin

39
Q

Which form of Hb has a higher affinity for O2, T or R?

A

R form

40
Q

What kind of allosteric modulator is O2 on Hb? What about 2,3-BPG, CO2 and H+?

A

O2 is a positive allosteric modulator of Hb, all the others are negative allosteric modulators of Hb

41
Q

CO2 can bind to N-terminal ends of Hb subunits and form carbamates, what effect will this have on the structure of Hb?

A

stabilizes T-form, facilitate release of O2 in peripheral tissues

Biochem Final (21 decks)

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