Brainscape's Knowledge GenomeTM

Browse over 1 million classes created by top students, professors, publishers, and experts.


See full index

CC 1 > 6. AMINO ACID ANALYSIS > Flashcards

6. AMINO ACID ANALYSIS Flashcards

1
Q

What fasting duration is required before blood sample collection for amino acid analysis?

A

6 to 8 hours

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

What type of tube is used for blood sample collection in amino acid analysis?

A

Green top (heparin) tube

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

What must be done within 30 minutes of blood sample collection for amino acid analysis?

A

Deproteinization

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

At what temperature should samples be frozen if there is a delay in amino acid analysis?

A

−20°C to −40°C

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

What is the primary purpose of deproteinization in amino acid analysis?

A

Removal of proteins

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

What type of urine sample is preferred for quantitation in amino acid analysis?

A

24-hour urine sample preserved with thymol or organic solvents

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

What method is used for screening in amino acid analysis?

A

Thin-layer chromatography

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

What process separates ions and molecules based on their affinity to ion exchangers?

A

Ion exchange chromatography

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

What kind of exchangers attract positively charged ions?

A

Cationic exchangers

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

What kind of exchangers attract negatively charged ions?

A

Anionic exchangers

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

What technique separates ions based on electrophoretic mobility using voltage?

A

Capillary electrophoresis

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

Which method in amino acid analysis is highly specific and sensitive?

A

Tandem Mass Spectrometry (MS/MS)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

What does MS/MS analyze by breaking down selected ions into fragments?

A

The chemical structure of precursor ions.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

What is the consequence of enzyme deficiencies in inborn errors of metabolism?

A

Accumulation of precursor substances

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

What accumulates in phenylketonuria due to the deficiency of phenylalanine hydroxylase?

A

Phenylalanine and its metabolites

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

What are proteins composed of?

A

Polymers of amino acids linked covalently through peptide bonds

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

Where are most proteins synthesized?

A

Liver

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

Where are immunoglobulins synthesized?

A

Plasma cells

19
Q

What are the primary elements found in proteins?

A

Carbon, oxygen, hydrogen, nitrogen, and sulfur.

20
Q

What is the primary structure of a protein?

A

Linear sequence of amino acids

21
Q

What determines a protein’s identity, functions, and molecular interactions?

A

primary structure.

22
Q

What forms the secondary structure of a protein?

A

α-helices, β-pleated sheets, and bend conformations.

23
Q

What adds strength and flexibility to proteins?

A

Secondary structure

24
Q

What describes the overall shape or conformation of a protein molecule?

A

Tertiary structure

25
Q

What structure results from the interaction of multiple protein subunits?

A

Quaternary structure

26
Q

What is the process called when a protein loses its shape and function?

A

Denaturation

27
Q

Name a cause of protein denaturation.

A

Heat, strong acids or alkali, enzymatic action, urea, ultraviolet light, or hydrolysis.

28
Q

Name a protein that catalyzes chemical reactions.

A

Enzyme

29
Q

Name a protein involved in glucose metabolism as a hormone.

A

Insulin, glucagon, growth hormone, or cortisol

30
Q

Name examples of enzymes.

A

Phosphatases, dehydrogenases, and transaminases.

31
Q

Name a transport protein.

A

Hemoglobin, albumin, or transferrin

32
Q

What type of protein mediates the humoral immune response?

A

Immunoglobulins

33
Q

What is an example of a structural protein?

A

Collagen, elastin, or keratin

34
Q

Name an example of a storage protein.

A

Ferritin

35
Q

Which protein helps maintain colloid osmotic pressure?

A

Albumin

36
Q

What database is used for structural classification of proteins?

A

SCOP (Structural Classification of Proteins)

37
Q

What is an example of a metalloprotein?

A

Ferritin

38
Q

What is a nucleoprotein found in eukaryotic cells?

A

Chromatin

39
Q

What is the basis for the Families of Structurally Similar Proteins (FSSP) database?

A

Three-dimensional protein structure

40
Q

Name a globular protein

A

Albumin or hemoglobin.

41
Q

Name a fibrous protein

A

Collagen or troponin

42
Q

What is a metalloprotein, and give an example?

A

A protein with a metal ion; examples are ferritin and ceruloplasmin.

43
Q

What is a glycoprotein, and give an example?

A

protein with carbohydrates; examples are haptoglobin and α-1-antitrypsin.

44
Q

What is a nucleoprotein, and give an example?

A

A protein linked to nucleic acids; an example is chromatin.

CC 1 (12 decks)

Brainscape helps you reach your goals faster, through stronger study habits.
© 2024 Bold Learning Solutions. Terms and Conditions