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CCFINALS > METHODS FOR TOTAL PROTEIN > Flashcards

METHODS FOR TOTAL PROTEIN Flashcards

1
Q

Classical method for protein quantitation

A

Kjeldahl Method

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2
Q

Reference method but not routinely used; TIME
CONSUMING

A

Kjeldahl Method

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3
Q

Kjeldahl Method

Measures the amount of __________ in specimen

A

Nitrogen

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4
Q

Kjeldahl Method

1 g of nitrogen = ?

A

6.54 g of proteins

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5
Q

Kjeldahl Method

3 STEPS:

A

a. DIGESTION
b. DISTILLATION
c. TITRATION

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6
Q

COMPONENTS OF THE PROTEIN:

A

CHON –
carbohydrate, oxygen and nitrogen

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7
Q

Measures protein based on the number of peptide
bonds present.

A

Biuret Method

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8
Q

Biuret Method

More peptide = ?

A

darker the color

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9
Q

The darker the color the more protein present in
the sample

A

Biuret Method

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10
Q

Biuret Method

The ______ present will bind to the peptide bonds
present in the protein forming

A

Copper

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11
Q

Biuret Method

peptide copper
complex = ?

A

violet

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12
Q

Most widely used method for total protein
determination

A

Biuret Method

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13
Q

Biuret Method

_______ because the end product has color
(“DEEP COLOR PURPLE”/VIOLET)

A

Colorimetric

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14
Q

Biuret Method

principle pr reagent do
not utilize enzyme

A

Non-enzymatic method

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15
Q

Biuret Method

Reagent consists:

A

a. Alkaline CuSO4
b. Sodium potassium tartrate (Rochelle
salt)
c. NaOH
d. Potassium iodide –

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16
Q

Biuret Method

Absorbance of color is read at ?

A

540 nm

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17
Q

Biuret Method

present in protein forms a
bond with cupric ions forming a violetcolored chelate.

A

Copper

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18
Q

Biuret Method

INTERFERENCE:

A

lipemic sample

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19
Q

Has the highest analytical sensitivity which
measures small concentration of protein

A

Folin-Ciocalteu (Lowry) Method

20
Q

Folin-Ciocalteu (Lowry) Method

Principle: ______ __ _________ ______ such as tyrosine, tryptophan, and histidine.

A

Oxidation of phenolic compounds

21
Q

Folin-Ciocalteu (Lowry) Method

tyrosine, tryptophan, and histidine to
give a ?

A

Deep blue color

22
Q

Folin-Ciocalteu (Lowry) Method

MOLYBDIC
ACID OR PHENOL REAGENT; oxidize phenolic
compounds

A

PHOSPHOTUNGSTIC

23
Q

Folin-Ciocalteu (Lowry) Method

the reagent will reduce which is
measured

A

spectrophotometrically

24
Q

Folin-Ciocalteu (Lowry) Method

Color enhancer:

A

BIRURET REAGENT

25
Q

The absorbance of proteins at 210nm is due to the
absorbance of the peptide bonds at specific
wavelength.

A

UV Absorption Method

26
Q

UV Absorption Method

Majority of proteins has absorbance of 210
except if there is ________ which is absorption at 280nm.

A

aromatic amino acid

27
Q

UV Absorption Method

tryptophan, tyrosine, and
phenylalanine absorption at ?

A

280nm

28
Q

based on measurement of
refractive index of serum total protein.

A

Refractometry

29
Q

Refractometry

Based how protein bend light and the
changes is ______ due to the
concentration of protein in the sample.

A

proportional

30
Q

Refractometry

More changes in light = ?

A

high protein in
sample

31
Q

Measurement
depends on formation of a uniform fine precipitate
which scatters incident light in suspension
(NEPHELOMETRY) or block light (TURBIDIMETRY).

A

Turbidimetry and Nephelometry

32
Q

used for detection of
proteins as little as 1 ug

A

Coomasie Brilliant Blue Dye

33
Q

develops violet color by reacting with
primary amines widely used for detection of peptides
and amino acids after paper chromatography

A

Ninhydrin

34
Q

Separation technique

A

Serum Protein Electrophoresis (SPE)

35
Q

Migration of charged particles in an
electric field

A

Serum Protein Electrophoresis (SPE)

36
Q

Serum Protein Electrophoresis (SPE)

cathode

A

Negative terminus electrode

37
Q

Serum Protein Electrophoresis (SPE)

anode

A

Positive terminus electrode

38
Q

Serum Protein Electrophoresis (SPE)

Protein will migrate in the anode because its ?

A

amphoteric

39
Q

Serum Protein Electrophoresis (SPE)

proteins charge is negative

A

Increase p H(basic)

40
Q

Serum Protein Electrophoresis (SPE)

the protein charge is positive

A

Decrease p H(acidic)

41
Q

Isoelectric Property of Proteins

either positive or negative
depending on pH condition

A

AMPHOTERIC

42
Q

Isoelectric Property of Proteins

ph where the
charge of protein is 0

A

No charge at ISOELECTRIC POINT

43
Q

The acidic and basic amino acids content of proteins
determines its net charge.

A

Isoelectric Property of Proteins

44
Q

Isoelectric Property of Proteins

amine and
carboxylic acid

A

Positive and negative component

45
Q

Isoelectric Property of Proteins

pH 8.6 which is basic

A

BARBITAL (VERONAL)

CCFINALS (8 decks)

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