for education purpose

2. HSA
• The protein is a monomer of 585 amino acid
residues
• Human Serum Albumin is synthesised and
secreted from the liver
• serves as a transport vehicle
• HSA displays an extraordinary ligand binding
capacity, providing a depot and carrier for
many endogenous and exogenous
compounds.

3. STRUCTURE
• one N-terminus, one C-terminus and three
homologous domains, named domain I,
domain II and domain III
• Each of these subdomains contains 4 to 6 α–
helices.
• HSA has 17 intramolecular disulfide bridges
that are present between the α-helices and its
stabilizes the HSA.

4. PQQ
• PQQ was readily released by denaturation of
the enzymes, and it was a red, highly polar,
acidic compound with a characteristic green
fluorescence.
• The fluorescence spectra of PQQ-containing
quinoproteins have a characteristic absorption
band between 300 and 420 nm.

10. 200 210 220 230 240
-200
-150
-100
-50
0
Ellipticity
Wavelength (nm)
HSA
0.5 equivalent of PQQ
1 equivalent of PQQ
free HSA molecule exhibited
two negative bands at 209 and
222 nm which correspond to
n → π* transition of peptide
bond and are typical of
proteins with α- helical
structure.