1997
DOI: 10.1016/s0162-0134(96)00147-x
|View full text |Cite
|
Sign up to set email alerts
|

Binding ability of Cu2+ ions by opiate-like fragments of bovine casein

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
3
1
1

Citation Types

0
11
0

Year Published

1998
1998
2011
2011

Publication Types

Select...
6

Relationship

2
4

Authors

Journals

citations
Cited by 11 publications
(11 citation statements)
references
References 7 publications
0
11
0
Order By: Relevance
“…The mechanism of relief of inhibition is not known, but it has been speculated (6) that stretches of phosphorylated serine residues present in bovine ␣-casein may be involved. These phosphorylated regions give bovine ␣-casein a high chelating force toward positively charged metal ions (3,11,27). This chelating power may be involved in the enhancing properties of bovine ␣-casein by capturing coextracted metal ions which might otherwise act as inhibitors of both RT and PCR.…”
Section: Discussionmentioning
confidence: 99%
“…The mechanism of relief of inhibition is not known, but it has been speculated (6) that stretches of phosphorylated serine residues present in bovine ␣-casein may be involved. These phosphorylated regions give bovine ␣-casein a high chelating force toward positively charged metal ions (3,11,27). This chelating power may be involved in the enhancing properties of bovine ␣-casein by capturing coextracted metal ions which might otherwise act as inhibitors of both RT and PCR.…”
Section: Discussionmentioning
confidence: 99%
“…The normal mode of coordination achieved in regular opiate-like peptides [15,16] is broken because Pro residues do not possess an ionizable peptide proton [67]. However, the presence of Pro residues promotes very stable dimeric species involving the Tyr side-chain phenolic donor.…”
Section: Tyr-d-ala-gly-phe-leu« (Cn 4 )Chmentioning
confidence: 99%
“…Therefore, the interactions between copper(II) ions and opioid peptides or their analogues were the focus of the reported work. The aim of reviewed studies was to investigate the coordinating effects of a new class of peptide chelators, tetrazole opioid peptide analogues [15][16][17][18][19][20][21][22], on copper(II) ions. The 1,5-disubstituted tetrazole ring is a cis amide bond surrogate [23][24][25][26].…”
Section: Introductionmentioning
confidence: 99%
See 1 more Smart Citation
“…The interaction of Cu(II) with these biomolecules may have physiological relevance because the copper content is high especially in synaptosomal fluids which are rich in opioid peptides [4]. Studies on the Cu(II)-exorphin systems have shown that these exogenous opiate-like peptides are efficient chelating agents [5][6][7]. Moreover, the insertion of the tetrazole ring can effectively stabilize the metallopeptide structure [8][9][10].…”
Section: Introductionmentioning
confidence: 99%