lab 2 Flashcards

1
Q

Techniques for purification procedures are often based on principles like

A

molecular size, electrostatic charge and solubility

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2
Q

With the development of affinity chromatography, it is possible to

A

achieve a high degree of purification in a single step

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3
Q

Affinity chromatography is based on

A

the ability of protein molecules to bind specifically and reversibly to appropriate ligands attached to insoluble supports

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4
Q

Ligands may be

A

competitive inhibitors, coenzymes, substrates, or their analogs

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5
Q

Colourimetric protein assays( such as _____, _____, and _____) are commonly used to measure

A

lowry, microbiuret, and bradford

the concentration of protein solutions because of their sensitivity and accuracy

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6
Q

The bradford method is preferred because

A

it is rapid and is not affected by most non-protein components

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7
Q

proteins and nucleic acids absorb in the UV range (_____) and show a peak at _____ for proteins and ______ for nucleic acids
The 280 peak for proteins in because of ______,_____ and _______

A

200-330
280
260
trptophan, tyrosine, and phenylalanine

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8
Q

The absorbance at 280 can be used to measure

A

The concentration of crude protein solutions

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9
Q

Absorbances at 215 nm provide what

but _____ will also absorb UV light

A

a very sensitive detection and measurement method for all proteins especially those with little or no trptophan
- the peptide bond

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