Copper(II) induced polymerization of human albumin, and its depolymerization by diglycyl-L-histidine: A pH static and ultracentrifugation study

Österberg, Ragnar; Braneg»rd, B.; Ligaarden, R.; Sarkar, Bibudhendra

doi:10.1016/s0006-3061(00)80057-5

Cited by 9 publications

(3 citation statements)

References 31 publications

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“…Unexpectedly, 0.5 mM CuCl2 complexed with 0.55 mM nitrilotriacetic acid, a soft chelator [24], increased specific [3H]progesterone binding to uteroglobin from 10000 to 40000 cpm/ml (table 3a). Copper 192 interacts with a histidine residue on albumin to promote its polymerization [45]. Analogously, copper could interact with histidine and/or cysteine on uteroglobin to stabilize the progesterone binding conformation.…”

Section: Effect Of Some Divalent Metal Ions Onmentioning

confidence: 99%

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Evidence that progesterone binding uteroglobin is similar to myosin alkali light chain

Baker

1985

FEBS Letters

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Using a computer program designed to detect evolutionary relationships between proteins, I find that exon 2 of rabbit uteroglobin, a progesterone binder, and part of myosin alkali light chain have a comparison score that is 7.2 standard deviations higher than that obtained with a comparison of randomized sequences of these proteins. The probability (p) of getting this score by chance is less than 10−12. This theoretical finding that these sequences are similar has led to the experimental finding that copper, calcium and the tranquilizer trifluoperazine, a calmodulin binding ligand, affect progesterone binding to uteroglobin.

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Section: Effect Of Some Divalent Metal Ions Onmentioning

confidence: 99%

“…The tranquilizer trifluoperazine binds to calmodulin with PM affinity [45]. Resins with covalently attached trifluoperazine are used to purify calmodulin by affinity chromatography.…”

Section: Effect Of Some Divalent Metal Ions Onmentioning

confidence: 99%

Evidence that progesterone binding uteroglobin is similar to myosin alkali light chain

Baker

1985

FEBS Letters

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“…Proposed structure of the main Cu(Il)-L-aspartyl-L-alanyl-L-histidine N-methylamide species (MH-2A) in the physiological pH range two tripeptide systems (Lau et al, 1974;Kruck et al, 1976). However, it is noteworthy that Cu(II) can induce aggregation of human serum albumin (Osterberg et al, 1975). Below pH5, another species, MA, is detected, which reaches a maximum of about 60 % of the total bound form at pH4.45.…”

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confidence: 97%

Synthesis of the native copper(II)-transport site of human serum albumin and its copper(II)-binding properties

Iyer¹,

Lau²,

Laurie³

et al. 1978

Biochemical Journal

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A derivative of the native-sequence tripeptide of the specific Cu(II)-transport site of human serum albumin, L-aspartyl-L-alanyl-L-histidine N-methylamide, was synthesized, and its binding to Cu(II) was examined to determine the influence of the side-chain groups on the Cu(II) binding. The equilibria involved in the Cu(II)-L-aspartyl-L-alanyl-L-histidine N-methylamide system were investigated by analytical potentiometry. Three complex species were found in the pH range 4-10. The same species were identified in both the visible and circular-dichroism spectra. The main species present in the physiological pH range is shown to have the same ligands around the square-planar Cu(II) ion as those reported for albumin and tripeptides diglycyl-L-histidine and its N-methylamide derivative. The results obtained from competition experiments showed that this tripeptide has a higher affinity towards Cu(II) than has albumin itself. The overall findings are compared with those from albumin. At neutral pH the side chains do not play any important role in the Cu(II) binding, but at low pH the beta-carboxyl group of the N-terminal aspartic residue becomes important. A possible competition site on albumin for Cu(II) at low pH is discussed.

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Copper and Hepatic Function

Owen

1980

Novartis Foundation Symposia

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Copper(II) induced polymerization of human albumin, and its depolymerization by diglycyl-L-histidine: A pH static and ultracentrifugation study

Cited by 9 publications

References 31 publications

Evidence that progesterone binding uteroglobin is similar to myosin alkali light chain

Evidence that progesterone binding uteroglobin is similar to myosin alkali light chain

Synthesis of the native copper(II)-transport site of human serum albumin and its copper(II)-binding properties

Copper and Hepatic Function

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