1.

1) Efficient extraction from biological material

2) Separation from non-protein components (nucleic acids
and lipids)
3) Precipitation steps, initially to recover the bulk protein
from a crude extract, followed by preliminary resolution
into manageable fraction
4) Use of ion exchange chromatography/size fractionation or
hydrophobic
chromatography columns to further separate
the target protein- containing fraction from the bulk protein
5) A more refined set of steps including an affinity matrix
to enable recovery of the target protein in a highly purified
state along with a high yield.
2.

a. Casein - this protein is commonly found in mammalian milk, making up 80% of

the proteins in cow milk and between 20% and 45% of the proteins in human milk.
b. Albumin -

- In quaternary structure denaturation, protein sub-units are

dissociated and/or the spatial arrangement of protein subunits is
disrupted.
- Tertiary structure denaturation involves the disruption of
covalent interactions between amino acid
side chains, non
covalent dipole-dipole interactions between polar amino acid side,
Van der interactions between nonpolar amino acid side chains.
- In secondary structure denaturation, proteins lose all regular
repeating patterns
- Primary structure, such as the sequence of amino acids held
together by covalent peptide bonds, is not disrupted by
denaturation.