Polypeptidyl derivatives of bovine pancreatic ribonuclease
(RNase) containing two or three tyrosine chains
with an average of two to three residues per chain have
been prepared. The effects of various perturbants such as
neutral salts, ethanol, urea and guanidine hydrochloride
on the thermal transition of the derivatives have been
studied....
In order to examine some possible tyrosyl interactions, poly-tyrosyl lysozyme and poly-O-methyltyrosyl lysozyme were prepared and their solubilities were compared. Both derivatives exhibited
similar pH dependent solubilities, showing a minimum solubility at
about pH 8. Their solubilities varied with temperature, having a
positive enthalpy of solution. The effect of a...
A comparative study was made on the effect of urea denaturation
of bovine serum albumin (BSA), polyglycyl BSA and poly-L-phenylalanyl
BSA. The denaturation process was followed by ultraviolet
spectrophotometry and optical rotation.
A blue shift in the absorption maximum at 278 mμ was observed
in urea denatured proteins, In 7M...
A heat stable derivative of bovine serum albumin containing
300 residues of glycine added to 30 sites on the surface of the protein
has been prepared. This derivative may be heated to 100° C for
prolonged periods of time without aggregation. By comparison,
native BSA aggregates at 62° C under...