Isolation and characterization of some fragments obtained after peptic digestion of bovine serum albumin.
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منابع مشابه
Isolation, Amino Acid Sequence and Copper (II) -binding Properties of Peptide (l-24) of Dog Serum Albumin*
The NH&erminal peptide fragment (l-24) of dog serum albumin was obtained by a limited peptic hydrolysis of whole albumin. The peptide fragment was isolated and subsequently purified to homogeneity by trichloroacetic acid fractionation, Sephadex gel filtration, and high voltage electrophoresis at pH 2.0. The purity of the peptide was established by 5-dimethylaminonaphthalene-I-sulfonyl (dansyl) ...
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, Amino Acid Sequence and Copper (II) -binding Properties of Peptide (l-24) of Dog Serum Albumin*
The NH&erminal peptide fragment (l-24) of dog serum albumin was obtained by a limited peptic hydrolysis of whole albumin. The peptide fragment was isolated and subsequently purified to homogeneity by trichloroacetic acid fractionation, Sephadex gel filtration, and high voltage electrophoresis at pH 2.0. The purity of the peptide was established by 5-dimethylaminonaphthalene-I-sulfonyl (dansyl) ...
متن کاملIsolation, amino acid sequence and copper(II)-binding properties of peptide (1-24) of dog serum albumin.
The NH&erminal peptide fragment (l-24) of dog serum albumin was obtained by a limited peptic hydrolysis of whole albumin. The peptide fragment was isolated and subsequently purified to homogeneity by trichloroacetic acid fractionation, Sephadex gel filtration, and high voltage electrophoresis at pH 2.0. The purity of the peptide was established by 5-dimethylaminonaphthalene-I-sulfonyl (dansyl) ...
متن کاملAffinity Chromatography of Serum Albumin with Fatty Acids Immobilized on Agarose*
Fatty acids immobilized on agarose have been employed in the isolation and study of serum albumin by affinity chromatography. Various oleyland palmityl-aminoalkylamino-agarose preparations bound about 10 mg of albumin per ml of agarose; other proteins were retained in smaller amounts and with lesser affinity. Fatty acid-agarose columns which had been exposed to human serum and then washed yield...
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عنوان ژورنال:
- International journal of protein research
دوره 3 5 شماره
صفحات -
تاریخ انتشار 1971