Exam Details
Subject | analytical techniques | |
Paper | ||
Exam / Course | b.sc. (biotechnology) | |
Department | ||
Organization | solapur university | |
Position | ||
Exam Date | March, 2018 | |
City, State | maharashtra, solapur |
Question Paper
B.Sc. (Biotechnology) II (Semester IV) (New CBCS) Examination, 2018
Analytical Techniques
Day and Date Monday, 7-5-2018 Max. Marks 70
Time 10.30 a.m. to 1.00 p.m.
Instructions All questions are compulsory.
Figures to right indicate full marks.
Draw neat and labeled diagrams.
1. Rewrite the following sentences by choosing correct alternatives. 14
Purpose of using gel is to Concentrate Proteins.
Stacking Separating Starch Agarose
Volume of per unit time is known as flow rate.
Stationary phase Mobile phase
Slurry Sample
Salting out is the process of of proteins in solution by the addition
of large amount of inorganic salt.
Agglutination Coagulation
Precipitation Dilution
Osmotic Shock is the method of cell disruption.
Enzymatic Chemical Analytical Physical
Usually in chromatography stationary phase is Water.
Paper TLC
Affinity Gel Permeation
is extensively used chromatographic technique to determine
base composition of nucleic acid.
GLC Ion exchange
Affinity Adsorption
ESI creates by holding a liquid at high potential difference.
Molecules Compound
Ions Fragments of molecules
Protein Expression Mapping involves study of global changes
in protein expression in cell or tissue.
Comparative Operative Qualitative Quantitative
In technique pH gradient in gel is used for separation.
IEF SDS-PAGE
Sedimentation PAGE
10) Dr. Willem Kolff constructed first working in 1943.
Capacitor Dialyzer Model Detector
11) is the most suitable gas to use as a carrier gas in GLC.
Carbon dioxide Oxygen
Helium Methane
12) are inversely proportional to Volatility of analyte in GLC.
Concentrations Volume of mobile phase
Volume of stationary phase Partition coefficients
13) Membrane proteins are during 2-D gel electrophoresis.
under represented Isolated
Lysed Clotted
14) invented 2-D gel electrophoresis independently in
1975.
Klose Muller O'Farrel Klose
Darvin Klose O'Farrel Muller
2. Answer the following (Any seven). 14
How will you prepare separating gel in SDS-PAGE
Explain the role of homogenizerin cell disruption.
How buffer affect electrophoretic mobility
Enlist the advantages and limitations of lowry assay.
Write a note on Introduction of proteomics.
Define isoelectric point.
Column used in column chromatography.
Write a note on chromatography.
Write the principle of Bradfoard assay.
3. Answer the following. (Any two) 10
Describe the ascending paper chromatographic technique.
How will you purify the proteins by dialysis
Discuss limitations of 2-D gel electrophoresis.
Describe assay used for iodine value. 4
4. Answer the following (Any two). 14
In which electrophoretic technique proteins get separated at its isoelectric
point.
Describe Edman degradation for protein sequencing.
Describe disc gel electrophoretic technique for protein.
5. Answer the following (Any two). 14
Give details of protein estimation by Bicinchonic acid.
Discuss chromatographic technique in which resins are used for ions.
Explain DNA blotting technique.
Analytical Techniques
Day and Date Monday, 7-5-2018 Max. Marks 70
Time 10.30 a.m. to 1.00 p.m.
Instructions All questions are compulsory.
Figures to right indicate full marks.
Draw neat and labeled diagrams.
1. Rewrite the following sentences by choosing correct alternatives. 14
Purpose of using gel is to Concentrate Proteins.
Stacking Separating Starch Agarose
Volume of per unit time is known as flow rate.
Stationary phase Mobile phase
Slurry Sample
Salting out is the process of of proteins in solution by the addition
of large amount of inorganic salt.
Agglutination Coagulation
Precipitation Dilution
Osmotic Shock is the method of cell disruption.
Enzymatic Chemical Analytical Physical
Usually in chromatography stationary phase is Water.
Paper TLC
Affinity Gel Permeation
is extensively used chromatographic technique to determine
base composition of nucleic acid.
GLC Ion exchange
Affinity Adsorption
ESI creates by holding a liquid at high potential difference.
Molecules Compound
Ions Fragments of molecules
Protein Expression Mapping involves study of global changes
in protein expression in cell or tissue.
Comparative Operative Qualitative Quantitative
In technique pH gradient in gel is used for separation.
IEF SDS-PAGE
Sedimentation PAGE
10) Dr. Willem Kolff constructed first working in 1943.
Capacitor Dialyzer Model Detector
11) is the most suitable gas to use as a carrier gas in GLC.
Carbon dioxide Oxygen
Helium Methane
12) are inversely proportional to Volatility of analyte in GLC.
Concentrations Volume of mobile phase
Volume of stationary phase Partition coefficients
13) Membrane proteins are during 2-D gel electrophoresis.
under represented Isolated
Lysed Clotted
14) invented 2-D gel electrophoresis independently in
1975.
Klose Muller O'Farrel Klose
Darvin Klose O'Farrel Muller
2. Answer the following (Any seven). 14
How will you prepare separating gel in SDS-PAGE
Explain the role of homogenizerin cell disruption.
How buffer affect electrophoretic mobility
Enlist the advantages and limitations of lowry assay.
Write a note on Introduction of proteomics.
Define isoelectric point.
Column used in column chromatography.
Write a note on chromatography.
Write the principle of Bradfoard assay.
3. Answer the following. (Any two) 10
Describe the ascending paper chromatographic technique.
How will you purify the proteins by dialysis
Discuss limitations of 2-D gel electrophoresis.
Describe assay used for iodine value. 4
4. Answer the following (Any two). 14
In which electrophoretic technique proteins get separated at its isoelectric
point.
Describe Edman degradation for protein sequencing.
Describe disc gel electrophoretic technique for protein.
5. Answer the following (Any two). 14
Give details of protein estimation by Bicinchonic acid.
Discuss chromatographic technique in which resins are used for ions.
Explain DNA blotting technique.
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- animal tissue culture
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- applications
- basics of molecular biology
- biochemistry
- bioenergetics and enzymology
- bioenergetics and enzymology (old)
- bioinformatics and nanotechnology
- biometry
- biophysical instruments
- biophysics
- biostatistics
- breakthrough
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- cell physiology
- chemical sciences
- computer science
- cytogenetics and population genetics
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- food and dairy technology
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- immunology – i
- immunology – ii
- inheritance biology
- introduction to biotechnology based industries
- mechanisms in immunology
- mechanisms in molecular biology
- metabolism (new)
- metabolism (old)
- microbial techniques
- microbiology
- molecular biology – i (old)
- molecular biology – ii
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- plant sciences
- plant tissue culture
- recent trends in biotechnology
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