A simple, sensitive, and quantitative method for the analysis of nonhistone chromosomal proteins separated by two-dimensional polyacrylamide gel electrophoresis was established. Chromosomal proteins were first fractionated by isoelectrofocusing gel electrophoresis. By this method the histones were f
The differentiation of fluorescamine-modified kinins by gel electrophoresis
β Scribed by A. Prakash; S. Roffman; L.M. Greenbaum
- Book ID
- 102627016
- Publisher
- Elsevier Science
- Year
- 1978
- Tongue
- English
- Weight
- 421 KB
- Volume
- 89
- Category
- Article
- ISSN
- 0003-2697
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β¦ Synopsis
A technically simple procedure has been found for the identification and differentiation of bradykinin, leukokinin-H, and lysyl-containing analogs of bradykinin. By reacting the kinins with fluorescamine and thus altering the charges, the modified kinins may be separated by polyacrylamide gel electrophoresis. At pH 4.2 fluorescamine-modified (FM) bradykinin may be separated from FM-leukokinin-H and from FM-Lys-bradykinin and FM-Met-Lys-bradykinin.
Similarly at pH 9.8, FM-Lys-bradykinin and FM-Met-Lys-bradykinin can be separated from FMbradykinin and FM-leukokinin-H.
FM-Lysyl-bradykinin and FM-Met-Lys-bradykinin are not separable at either pH. This procedure may prove to be extremely useful in the identification and purification of kinin peptides.
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