Cyanogen Bromide Fragments of Human Serum Albumin
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چکیده
منابع مشابه
Binding and relaxometric properties of heme complexes with cyanogen bromide fragments of human serum albumin.
The spectroscopic and reactivity properties of hemin complexes formed with cyanogen bromide fragments B (residues 1-123), C (124-298), A (299-585), and D (1-298) of human serum albumin (HSA) have been investigated. The complex hemin-D exhibits binding, spectral, circular dichroism, and reactivity characteristics very similar to those of hemin-HSA, indicating that fragment D contains the entire ...
متن کاملImmunochemical cross-reactivity between cyanogen bromide fragments of human serum albumin.
The antigenic structure of human albumin was investigated in order to establish whether or not there was any similarity between its antigenic sites. Using immunoadsorbent columns prepared with cyanogen bromide fragments of human serum albumin, antibodies directed against different portions of the albumin molecules were isolated. Measurement of the amount of the antibodies isolated and study of ...
متن کاملHemocompatibility evaluation for peptide fragments of human serum albumin cleaved by cyanogens bromide.
We have previously demonstrated that peptide fragments of human serum albumin can be developed into potential renal targeting drug carriers. However, the interactions of these peptide fragments with red blood cells and plasma components are not evaluated well and there is yet no report on the evaluation of the hemocompatibility of peptide fragments. In this study, three kinds of peptide fragmen...
متن کاملLarge fragments of human serum albumin.
Large fragments of human serum albumin were produced by treatment of the native protein with pepsin at pH3.5. Published sequences of human albumin [Behrens, Spiekerman & Brown (1975) Fed. Proc. Fed. Am. Soc. Exp. Biol. 34, 591; Meloun, Moravek & Kostka (1975) FEBSLett.58, 134-137]were used to locate the fragments in the primary structure. The fragments support both the sequence and proposed dis...
متن کاملIsolation and Characterization of the Cyanogen Bromide Glycopeptide Fragments of cr-1-Antitrypsin”
cy-1-Antitrypsin can be cleaved by cyanogen bromide and separated on a column of Sephadex G-50 into a glycopeptide-containing fraction and four to seven carbohydrate-free peptides. The void volume fractions containing the glycopeptides can be resolved further into four unique glycopeptides (A, B, C, and D) by ion exchange chromatography on DE62 cellulose by elution with increasing concentration...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1971
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)61998-2