منابع مشابه
Limited pepsin digestion of human plasma albumin.
Limited pepsin digestion of human plasma albumin at pH 3.5 and 0 degrees in the presence of octanoate caused cleavage at residue 307 of the albumin molecule to yield two fragments. Thw two fragments corresponding to the NH2- and the COOH-terminal halves of the molecule were isolated in yields of about 15%. The COOH-terminal fragment is a mixture in which about 85% of the molecules had an additi...
متن کاملHydrogen Ion Concentration and Pepsin Digestion
One of the most striking peculiarities of enzyme action is the fact that the activity of the enzyme is limited to a definite range of acidity. If the solution is more or less acid than this the enzyme is practically inactive. SSrensen 1 showed that for a number of enzymes the determiuing factor was the hydrogen ion concentration and not the total acidity of the solution. In attempting to accoun...
متن کاملPepsin Digestion of Rabbit and Sheep Antibodies
7S sheep antibody is similar to 7S rabbit antibody, insofar as it too can be digested with pepsin to yield a 5S fragment still capable of precipitating homologous antigen. The 5S fragment from rabbit as well as sheep antibody is capable of fixing guinea pig complement. However, this fixation differs from the fixation by 7S antibody, since preformed antibody-antigen aggregates containing either ...
متن کاملComplete antibody digestion with pepsin in just three minutes
Capturem Pepsin was developed for rapid and efficient digestion of antibodies—with a room-temperature protocol (Figure 1)—designed for downstream proteomics analysis. Pepsin is an acidic protease with utility in a wide variety of applications, most notably in antibody sample preparation for characterization by mass spectrometry (MS). The specificity (Keil, B. 1992) and activity of digestion are...
متن کاملStructure of an Exophthalmos-producing Thyrotropin by Partial Pepsin Digestion
Previously reported experiments (Winand, R. J., and Kohn, L. D. (1970) J. Biol. Chem. 245, 967-975; Kohn, L. D., and Winand, R. J. (1971) J. Biol. Chem. 246, 6570-6575) have demonstrated that partial pepsin digestion of bovine thyrotropin preparation yields a fragment of the thyrotropin molecule which is exophthalmogenic but has negligible or no thyroid-stimulating activity. In the present repo...
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ژورنال
عنوان ژورنال: Molecular & Cellular Proteomics
سال: 2011
ISSN: 1535-9476
DOI: 10.1074/mcp.m110.001479