Acid Base Equilibrium Flashcards

1
Q

Most important biological buffers?

A

Phosphate
Bicarbonate
Proteins

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2
Q

Buffers consist of:

A

Weak acid and its conjugate base that are in equilibrium

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3
Q

The difference between strong and weak acids?

A

Weak acids are not completely dissociated under conditions within the biological system

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4
Q

Benefit of Henderson-Hasselbalch equation?

A

calculation of the amounts of undissociated acid and its conjugated base at any PH

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5
Q

Change of 1 pH unit results in? “Hassel equation”

A

10-fold change in the ratio of acid to conjugate base

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6
Q

Titration?

A

The addition of a strong acid to a weak base, or a strong base to a weak acid for the purpose of buffering the solution (maintaining pH)

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7
Q

Buffering capacity depends on 2 factors?

A
  1. The concentration of the buffer

2. Its pH

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8
Q

The buffer is most effective when the……. equals …….

A

pH , pKa

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9
Q

The buffer in plasma and interstitial fluid is………

While in the intracellular fluid is……..

A

Bicarbonate,

Phosphate and proteins

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10
Q

Hemoglobin is a good buffer because of?

A

The presence of Histidine

* It is a basic amino acid

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11
Q

What makes carbonic acid a strong buffer?

A

The ability of the acid to convert to carbon dioxide

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12
Q

Normal pH of blood plasma is?

A

7.4

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13
Q

Acidosis results from?

A
  1. Hypoventilation (respiratory acidosis)

2. Accumulation of lactic acid, acetoacetic acid and beta hydroxybutyric acid (metabolic acidosis)

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14
Q

Alkalosis results from?

A
  1. Hyperventilation (respiratory alkalosis)

2. Loss of stomach acids (metabolic alkalosis)

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15
Q

Phosphate buffer is of little importance in plasma?

A

Because of its low concentration in ECF

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16
Q

Phosphate buffer is important in?

A

Red blood cells and kidney tubules

17
Q

Why proline differs from the rest of the amino acids?

A

because the side chain forms a cyclic structure with the amino group

18
Q

Histidine is the the only amino acid with good buffering capacity. True/False?

A

True.. Because easily and reversibly accepts and donates protons.
* The imidazole side chain of histidine has a pKa of 6.5 (pKa is withing the physiologic pH range, means a good buffer)

19
Q

In general, the protein folds so that the ….. is to the out side of the molecule.

A

the hydrophilic side chain

20
Q

Hydrophobic aminoacids have …….. or ……. groups within the side chains

A

aliphatic or aromatic

21
Q

Hydrophilic side chains contain?

A

S, O or N atoms

22
Q

Serine and threonine have uncharged side chain containing……….

A

Hydroxyl groups

23
Q

Cysteine side chain contains……….

A

sulfur

24
Q

Asparagine and glutamine side chains have…..

A

amide groups

25
Q

Cystine is formed by………. . Its function is …….

A
  1. disulfide linkage between two cysteines (the only covalent cross linkage in proteins)
  2. stabilize the 3 dimensional structure of extracellular proteins
    * Abundant in Insulin and Ig
26
Q

Post translational modification is ?

A

modification of common amino acids after the protein has been synthesized.

27
Q

Hydroxyproline is formed by…….. in ……… where it functions as………

A
  1. O2 dependent hydroxylation of proline
  2. Fibroblasts
  3. stabilization of the triple helical structure of collagen

436

28
Q

Phosphotyrosine, phosphoserine and phosphothreonine are formed by…… and function for…….

A
  1. transferring a phosphate from ATP to hydroxyl group

2. signal transduction

29
Q

why glycine is differenet

A

the alpha carbon is connected to a hydrogen atom as a side chain

30
Q

Which stereoisomer is incorporated in proteins?

A

L-amino acids

31
Q

Define PI?

A

isoelectric point. The pH where the a molecule is not charged (neutral)

32
Q

Define Zwitterion

A

The protein that has both positive and negative charge at neutral pH
* Glycine has a net negative charge at any pH above its isoelectric point, so it moves toward the positive electrode. At any pH below its isoelectric point (pI), glycine exhibits a net positive charge and moves toward the negative electrode