Studies of copper(II) binding to glycylglycyl-l-Tyrosine-N-methyl amide, a peptide mimicking the NH2-terminal copper(II)-binding site of dog serum albumin by analytical potentiometry, spectrophotometry, CD, and NMR spectroscopy-Reference-Cited by-同舟云学术

Studies of copper(II) binding to glycylglycyl-l-Tyrosine-N-methyl amide, a peptide mimicking the NH2-terminal copper(II)-binding site of dog serum albumin by analytical potentiometry, spectrophotometry, CD, and NMR spectroscopy

Published:1984-01 Issue:3 Volume:21 Page:215-226
ISSN:0162-0134
Container-title:Journal of Inorganic Biochemistry
language:en
Short-container-title:Journal of Inorganic Biochemistry

Author:

Muller Daniel,Révérend Brigitte Decock-Le,Sarkar Bibudhendra

Publisher

Elsevier BV

Subject

Inorganic Chemistry,Biochemistry

Reference36 articles.

1. The State of Copper in Human Serum: Evidence for an Amino Acid-bound Fraction *

2. Evidence for albumin – Cu(II) – amino acid ternary complex

3. Copper-binding Properties of Bovine Serum Albumin and Its Amino-terminal Peptide Fragment

4. The Thermodynamics of Metallo-protein Combinations. Copper with Bovine Serum Albumin

5. A STABLE EQUIMOLAR COPPER(II)-ALBUMIN COMPLEX

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