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X = ~. X = ~. X = 7.. X = !!. OJ HMH .. (3 000000; (55 600; -6·50) (209000; -7 '24) , (4180000 ; -9'01 ) M (5800000; -9·20) 0 HOLES, HANDEDNESS, HANDLES, AND HOPES 47 In the remainder of this article, the stability constants for complex formation_yith Me3CNH3+SCN- will be quoted in parentheses as Ka values in M together with the derived free energies of complexation (~G) in kcal mol- l after each crown compound for which values have been reported. The format (K a , ~G) will be adopted for the presentation of this data.

327-349. S. Chern. , p. 481 and references cited therein. : 1967, J. Arn. Chern. Soc. 89, p. 2495, 7017. : 1972, Angew. Chern. 84, p. 16 and references cited therein. : 1973, Tetrahedron 29, p. 1629. S. Chern. , p. 1055. S. Chern. , p. 15. : 1976, Helv. Chirn. Acta 59, p. 1566. S. Chern. , p. 393. : 1976, Heterocycles 5, p. 477. : 1977, J. Am. Chern. Soc. 99, p. 6766. : 1978, J. Am. Chern. Soc. 100, p. 4914. S. Chern. , p. 487. S. Chern. , p. 1100. : 1973, Angew. Chern. 85, P•. 621,622; 1977, Nouveau J.

0 Ni/HSA Figure 2. Distribution of supernatant Ni(II) as percentage of total Ni(II) after ultracentrifugation at various Ni(II): albumin ratio. Native serum, 0---0; Dialyzed serum + amino acids, + - - - +; Dialyzed serum, ,~. ; Albumin + amino acids, ---.. Also L-histidine was shown to possess a greater affinity for Ni(II) than albumin does. The typical U shaped curve seen in Fig . 3 is the result of a competition between L-histidine and albumin for Ni(II)-binding. The albumin binding to Ni(II) becomes evident only when no more L-histidine is available for Ni(II)-binding.

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