(NO TITLE).
Abstract
Studies of the catalytic protein waves were extended to protein solutions containing guanidine hydrochloride. The waves of guanidine denatured albumin are much higher while those of irradiation denatured albumin are lower than that of a native albumin solution. The explanation is that the albumin molecule may have different structures if subjected to different methods of denaturation. This is substantiated by viscosity measurements of untreated and guanidine denatured albumin before and after UV irradiation. Fission of disulfide groups under the action of UV light has little effect on the reduced viscosity while fission by means of reducing agents in guanidine denatured albumin results in relatively large changes in viscosity. Interesting results were obtained with irradiated albumin solutions in the presence of various amounts of HgCL2 which acts as a sulfhydryl blocking agent. In the presence of the latter more Hg can be bound by albumin after irradiation. Radiation effects on solutions of mercaptoethylamine, mercaptoethylguanidine and aminoethanethiosulfuric acid were determined. (Author)
Document Details
- Document Type
- Technical Report
- Publication Date
- Feb 01, 1964
- Accession Number
- AD0432867
Entities
Organizations
- Marquette University