Biochem Exam 2 Flashcards

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1
Q

Branched Chain Ketoacid Dehydrogenases

A

break down the products of Val, Leu, and Ile E1 reactions (the toxic ketoacid)

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2
Q

MSUD- Maple Syrup Urine Disease

A

Absence of Branched Chain Ketoacid Dehydrogenase
Ketoacid builds up and is excreted in the urine
Can be a deadly disease.

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3
Q

Kidney Pressure Filtration

A

Blood pressure forces small molecules from the glomerulus into the Bowman’s capsule
-Water, glucose, amino acids, salts, urea, uric acid, and creatinine are transported from capillaries to kidneys

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4
Q

Kidney Selective Reabsorption

A

Diffusion and active transport return molecules to blood at the proximal convaluted tubule
–Bicarbonate HCO3 is put back into blood stream if pH is low and reabsorbed if it is high

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5
Q

Kidney Tubular Secretion

A

Active transport moves molecules from blood into the distal convoluted tubule

  • -waste is sent back to the kidney
  • -H+ is secreted from blood to kidney and appears in the urine if pH is low in the blood
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6
Q

Kidney Reabsorption of water

A

Along the length of the nephron and notably at the loop of Henle and collecting duct, water returns by osmosis following active reabsorption of salt

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7
Q

Hormone controlling water absorption

A

ADH- antidiuretic hormone
retain H2O in body by promoting waters removal back into the tissue fluids from last part of the nephron (vasopressin)
-Alcohol prevent the release of ADH, causing frequent urination and dehydration

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8
Q

Acidosis

A

decrease in blood pH

-Causes: starvation, diabetes, pulmonary disease

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9
Q

Alkalosis

A

increase in blood pH

-Causes: prolonged vomiting, excessive consumption of basic medicines, hyperventilation

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10
Q

Job of the Kidneys

A

Controls the pH of the blood by:

  • Low pH: the specialized cells excrete proteins from the blood to the urine; reabsorb bicarbonate into the kidney capillaries
  • High pH: do not secrete proteins from the blood, do not reabsorb bicarbonate into the kidney capillaries
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11
Q

Respiratory Control

A

Drop in pH: increate rate and depth of breathing to expel more carbon dioxide.

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12
Q

Chemical buffer system (Kidneys)

A

a. Bicarbonate buffer
b. Protein buffer system
c. Hemoglobin
d. Phosphate buffer

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13
Q

Phosphate buffer

A

Intracellular fluid and urine buffer

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14
Q

Hemoglobin

A

Red blood cell protein buffers the protons by metabolically producing carbon dioxide. This carbon dioxide dissociates to form bicarbonate, which is bound to hemoglobin to lower pH.

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15
Q

Protein buffer system

A

Proteins can give up protons, thus buffering

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16
Q

Bicarbonate buffer

A

the primary buffer of the extracellular fluid. Buffers against pH changes from fluctuation in carbon dioxide-generated carbonic acid.

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17
Q

Extracellular fluid

A

Plasma & interstitial fluid

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18
Q

Three sources of added H+

A
  1. Carbonic acid from metabolically produced Carbon Dioxide
  2. Acids produced from the breakdown of nutrients in the diet
  3. Acids produced from normal metabolism (like lactic acid from oxidized glucose)
19
Q

Equation for making carbonic acid in the blood

A

Glucose +O2 > CO2 +H2O > H2CO3

20
Q

Signs of Respiratory Acidosis

A
  • Emphysema
  • Chronic Bronchitis
  • Pneumonia
  • Asthma
  • Overdoes of Opioids or sleep meds
21
Q

Signs of Alkalosis

A

Metabolic: prolonged vomiting, excessive ingestion of basic compounds (baking soda, etc)
Respiratory: Hyperventilation (system tries replenishing CO2)

22
Q

The Pancreas

A

sends bicarbonate to small intestine to increase pH for pancreatic enzymes to work in the acidic chyme from the stomach

23
Q

Antifreeze

A

Ethylene glycol > Gycolic Acid > oxalic acid > oxylate + Calcium > CaC2O4 precipitates in kidneys causing kidney failure

24
Q

Radical Mutation

A

A change causing the amino acid to be changed to something not similar to the original

25
Q

Conserved Mutation

A

A change causing a new, but similar amino acid

26
Q

Apoptosome

A

A chemical of the cell present and needed in preparation for apoptosis

27
Q

Chymotrypsin

A

Carboxyl side of the Phe, Tyr, Trp

  • Created by the pancreas and active in the small intestine
  • If active prematurely, will cause pancreatitis
28
Q

Trypsin

A

Carboxyl side of Lys and Arg (the most basic AAs)

29
Q

Staphylococcus V8 protease

A

Carboxyl side of Glu, Asp (the most acidic AAs)

30
Q

Staphylococcus V8 protease plus Bicarbonate

A

Carboxyl side of Glu only

31
Q

Aminopeptidase

A

w/in peptide chain and starts at the Amine terminal

32
Q

Carboxypeptidase

A

Cleaves at Carboxyl terminal

33
Q

CNBr Treatment

A

Carboxyl side of Met

-Homoserine lactone derivative is formed

34
Q

Hydrazine (N2H4) Treatment

A

Derivatives all AA except the Carboxyl terminal AA, allowing it to be identified chromatographically

35
Q

PITC (Edman’s Reagent)

A

Phenylisothiocyle (?)

  • derivates end terminous
  • Ring-N+C+S
36
Q

FDNB (Sanger’s Reagent)

A

1-fluoro-2,4-dinitrobenzene

  • Reacts/derivates/identifies N terminal
  • Removes F and 2H, and attaches at H3N
37
Q

2-Dimensional Eletrophoresis

A

Take gel from isoelectric tube, separated by pI; then place on flat gel to separate by molecular weight

38
Q

Beta-mercaptoethanol

A

For reducing disulfide bonds (breaking)

–Cysteine bonds keep proteins together by covalent interactions, which SDS cannot breat

39
Q

Isoelectric focusing

A

separates by pI

40
Q

Dithiotheritol

A

reduces/breaks sulfide bonds (like of cysteine bonds)

41
Q

Multimeric proteins

A

composed of several distinct polypeptides

42
Q

Affinity Chromatography

A
  • most selective due to an immobilized ligand
  • some proteins will have an affinity for the ligand and get stuck to the column
  • to remove bound protein, change the mobile phase to an unbound ligand
43
Q

Non-denaturing electrophoresis (PAGE)

A

all proteins folded in their active shape that separate by weight, shape, and ionization

44
Q

Denaturing electrophoresis (SDS-PAGE)

A
  • aka polyacrylomide gel electrophoresis

- Binds along the backbone of proteins causing (-) charge and unfolding