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Binding of cupric ions to bovine serum albumin

✍ Scribed by Datta V. Naik; Charles F. Jewell Jr.; Stephen G. Schulman

Publisher: John Wiley and Sons
Year: 1975
Tongue: English
Weight: 322 KB
Volume: 64
Category: Article
ISSN: 0022-3549
DOI: 10.1002/jps.2600640729

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✦ Synopsis

The binding of cupric ions to bovine serum albumin was investigated by using a cupric-ion-specific electrode. When using a modified form of the Scatchard equation, it was determined that there are at least two classes of binding sites on bovine serum albumin for cupric ions. One class has three binding sites of relatively strong affinity, with an average binding constant of 3.0 X lo6. The other class has about 16 binding sites of relatively weak affinity, with an average binding constant of 2.0 X 104.

Keyphrases 0 Cupric ions-binding to bovine serum albumin, determination of number and classes of binding sites, specific ion electrode 0 Copper-protein binding interactions-studied using specific ion electrode 0 Serum protein binding-binding of cupric ions to bovine serum albumin, studied using specific ion electrode ' All compounds were analyzed for their carbon, hydrogen, and nitrogen content. Melting points were taken in open capillary tubes with partial immersion thermometer and are corrected.

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