منابع مشابه
The Isoelectric Point of Adsorbed Hemo- Globin*
It is well established that various proteins, as gelatin and albumin, can be adsorbed on various adsorbents so that the proteincoated particle of adsorbent behaves electrophoretically as a particle of protein (Loeb, 1923; Freundlich and Abramson, 1928). Dummett and Bowden (1933) have recently reported, however, that the behavior of adsorbed hemoglobin varies with the adsorbent surface. Thus, wh...
متن کاملThe isoelectric point of bacterial cells.
This study was undertaken to compare the isoelectric points of gram positive and gram negative bacterial cells by the method of microelectrophoresis. Within recent years a number of workers have referred to differences in the isoelectric point of the gram positive and the gram negative groups of bacteria. This concept arose from the studies of Stearn and Steam (1924, 1925, 1928), Tolstoouhov (1...
متن کاملPIP-DB: the Protein Isoelectric Point database
UNLABELLED A protein's isoelectric point or pI corresponds to the solution pH at which its net surface charge is zero. Since the early days of solution biochemistry, the pI has been recorded and reported, and thus literature reports of pI abound. The Protein Isoelectric Point database (PIP-DB) has collected and collated these data to provide an increasingly comprehensive database for comparison...
متن کاملIsoelectric Point Separations of Peptides and Proteins
The separation of ampholytic components according to isoelectric point has played an important role in isolating, reducing complexity and improving peptide and protein detection. This brief review outlines the basics of isoelectric focusing, including a summary of the historical achievements and considerations in experimental design. Derivative methodologies of isoelectric focusing are also dis...
متن کاملRelationship between isoelectric point of native and chemically modified insulin and liposomal fusion.
Native insulin causes fusion of negatively charged liposomes in the pH range from 3.0 to 5.5. In marked contrast, insulin with all three amino groups succinylated did not show fusion ability at any pH. On the other hand, insulin amidated with glycine methyl ester with all six carboxyl groups blocked shifted its activity to higher pH, showing a pH range of activity from 3.0 to 7.4. When the carb...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1933
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)76023-7