Module 5 Flashcards

(50 cards)

1
Q

a chemical test that can be used to check for the presence of peptide bonds in each analyte

A

biuret test

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1
Q

be used to gauge the amount of protein present in the analyte

A

biuret test

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2
Q

this test, the presence of peptides results in the formation of pale purple colored (or mauve colored) coordination compounds of the copper(II) ion (when the solution is sufficiently alkaline)

A

biuret test

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3
Q

Principle for Biuret Test

A

Alkaline CuSO4 reacts with compounds containing two or more peptide bonds to give a violet-colored product which is due to formation of co-ordination complex of cupric ions with un-shared electron pairs of peptide nitrogen and O2 of water.

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4
Q

Reagents for Biuret Test

A
  • 10% Sodium Hydroxide
  • 0.5% Copper Sulfate
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5
Q

Test Solutions for Biuret Test

A

Test Solutions for Biuret Test

  • 5% Albumin
  • 5% Arginine
  • 5% Glycine
  • Distilled Water
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6
Q

What is the positive and Negative result for Biuret test?

A

Positive = Purple
Negative = Blue

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7
Q

the only amino acid that give biuret test positive

A

Histidine

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8
Q

What ions can interfere in a biuret test?

A

magnesium and ammonium ions

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9
Q

True or false? Presence of magnesium and ammonium ions can be overcome by using excess alkali.

A

True

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10
Q

 A high concentration of ammonium salts and bile pigments influences the reaction.
 It is not as sensitive as the Folin Lowry test

A

Limitations of the Biuret Test

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11
Q

What are the functions of proteins?

A

Catalysis, Defense, Transport, Signaling, Movement, Structure

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12
Q

Enzymes that speeds up chemical reaction

A

Catalysis

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13
Q

Antibodies and complement proteins move the cell or molecules with the cell

A

Defense

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14
Q

Protein binds and transport numerous small molecules and ions through the body

A

Transport

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15
Q

Proteins that conveys signals between cells

A

Signaling

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16
Q

Motor and contractile protein move the cells or molecules within the cell

A

Movement

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17
Q

Structure proteins define cell shape and comprise body structures

A

Structure

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18
Q

They are linear in shape

A

Fibrous Protein

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19
Q

Spherical or globular in shape

A

Globular Protein

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20
Q

composed only of amino acids

A

Simple Protein

21
Q

composed of amino and non
amino acid component

A

Conjugated Protein

22
Q

what are the three ways to classify proteins?

A

structure, composition and function

23
Q

is a biochemical test for the detection
of amino acids containing phenolic or indolic groups like phenylalanine, tyrosine, and tryptophan (aromatic amino acids)

A

Xanthoproteic test

24
The test is named Xanthoproteic test due to the formation of a
yellow precipitate of xanthoproteic acid
25
Concentrated nitric acid reacts with the phenyl ring to give a yellow-colored aromatic nitro compound. Addition of alkali at this point will deepen the color to ______.
orange
26
What are the reagents for the Xanthoproteic test
* Nitric acid * 40% NaOH
27
What are the test solutions for the Xanthoproteic
* 1% tyrosine * 1% tryptophan * 1% phenylalanine * 5% egg white * Distilled Water
28
What is the result for a negative xanthoproteic test?
No dark yellow or orange color
29
What is the result for a positive xanthoproteic test?
Dark yellow or orange color present
30
The test allows the differentiation of aromatic amino acids from non-aromatic amino acids.
xanthoproteic test
31
Why doesnt phenylalanine give a positive xanthoproteic test despite being an aromatic group containing amino acid?
phenylalanine has a highly stable phenyl group
32
a chemical test performed to detect the presence of ammonia, primary/secondary amines, or α-amino acids.
Ninhydrin test
33
This test involves the addition of ninhydrin reagent to the test sample that results in the formation of deep blue color, often termed as Ruhemann’s purple, in the presence of an amino group
Ninhydrin test
34
what is the principle of the ninhydrin test
Amino acids with a free NH2 group and proteins containing free amino groups react with ninhydrin to give a purple-blue complex.
35
In amino acids like proline and hydroxyproline, ninhydrin test yields an iminium salt which is
yellow-orange
36
proteins with a free amino group like asparagine, react with the ninhydrin reagent to form a
brown colored product
37
what are the reagents in a ninhydrin test
2% ninhydrin solution
38
what is the test solutions for a ninhydrin test
* 1% alanine * 1% asparagine * Distilled Water
39
what is the preparation of 2% ninhydrin solution
0.2g of ninhydrin in 10ml of acetone or ethanol
40
* Also known as the glyoxylic acid reaction * Used for detecting the presence of tryptophan, the only amino acid containing an indole group. * The indole ring reacts with glyoxylic acid in the presence of a strong acid to form a violet cyclic product.
Hopkin's Cole test
41
what is the principle of the Hopkins Cole test
tryptophan reacts with glyoxylic acid in the presence of a strong acid to form a violet cyclic product
42
What is the negative and positive result for a hopkins cole test
Negative = no purple ring, tryptophan absent Positive = purple ring present, tryptophan present
43
True or False? In the hopkins cole test compounds like nitrites, chlorates, nitrates, and excess chlorides prevent the formation of the condensation product.
True
44
* a biochemical test consisting of colorimetric reaction for the detection and quantification of guanidinium groups. * used as a qualitative test for arginine that is either free or in protein. *a specific test for arginine where the guanidinium group of arginine reacts with 1-naphthol or α-naphthol to produce a colored product.
Sakaguchi test
45
What are the reagents in the sakaguchi test
* 1% alpha naphthol * 10% Sodium hypobromite solution of bromine water * 40% NaOH
46
what are the test solutions in the sakaguchi test
* 1% arginine * 1% glycine * 5% albumin * Distilled Water
47
what is the positive and negative result for the sakaguchi test
Negative = No red color complex (arginine or guanidium compound absent) Positive = Presence of red colored complex (arginine or guanidium compound present)
48
How can a sakaguchi test be made quantitative?
the addition of urea
49
what can cause difficulties in the testing results of the sakaguchi test
some of the guanidium groups in the solution might be destroyed by the hypochlorite, resulting in difficulties in testing results