THE ISOELECTRIC POINT OF ADSORBED HEMOGLOBIN
نویسندگان
چکیده
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...
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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...
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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...
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Capillary isoelectric focusing (cIEF) was used to identify and quantify major and minor hemoglobin (Hb) variants. Whole blood (approximately 10 microL required) hemolysate was analyzed with a commercial instrument equipped with a 50 microns (i.d.) x 27 cm coated capillary filled with 20 g/L ampholytes (pH 6-8) in 4 g/L methylcellulose (MC). Cathode and anode solutions were 20 mol/L NaOH and 100...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1936
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)74855-2