Keratin Derivatives Extracted From Wool with Alkaline Thioglycollate Solutions

Abstract

In extension of previous work (Gillespie and Lennox 1953), the conditions under which proteins may be extracted from washed Merino wool have been further examined. Approximately 65 per cent. of the wool can be dissolved by a 40-min extraction at 50°C with O·1M thioglycollate at an initial pH of 12· 6. Electrophoresis at pH 11 in thioglycoIlate-glycine buffer indicated the presence of seven minor and one major component, the latter amounting to 41 per cent. of the wool. The minor components can be completely removed from the wool by five 2,O-min extractions with O·1M thioglycollate at an initial pH of 10·5. Extraction of the residue at pH 12·3 yields the major component. This moves as a single peak on electrophoresis between pH 8·0 and 12·0 in the presence of various buffers. It has a mobility of -7·2 X 10-5 cm2 V-I sec- I at a protein concentration of 0·5 per cent. in thioglycollate-glycine buffer of ionic strength O· 22 at pH 11· O. At higher protein concentrations there is anomalous behaviour on the descending boundary and tills can be prevented by increasing the ionic strength or replacing thioglycollic acid with mercapto-ethanol. The ascending pattern is unaltered by these changes or by increased protein concentration.