St&is of Peptide Analogues of the Copper( Transport Site of Dog Serum Albumin
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چکیده
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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 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) ...
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Metal binding strategies employing low molecular weight chelators and equilibrium dialysis were used to investigate several unresolved aspects of zinc and copper binding to serum albumin. Direct measurement of histidine binding to bovine serum albumin when the histidine is presented either as a metal-chelate or alone provides no evidence for an albumin-metal-histidine ternary complex. Using pre...
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Diglycyl-L-histidine is a peptide molecule designed to mimic the specific Cu(II) transport site of human albumin. The equilibria involved in the Cu(II)-diglycyl-L-histidine system have been investigated by analytical potentiometry in aqueous solution (0.15 M NaCl, 25’). The synthetic peptide molecule bound Cu(I1) exclusively as a 1: I complex in the pH range of 6.50 to 11.00. The results furthe...
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