Metals in biochemistry : P.M. Harrison and R.J. Hoare,Chapman & Hall,New York, 1980, 80 pp. $5.95 (paper)

An ultrafiltration technique was used to study stripping by glycine of the first copper and zinc ion equivalents bound by bovine, dog, and rat serum albumins at pH 7.5. Affinity of dog serum albumin for copper was poorer than for the other albumins, consistent with the absence in the former albumin of the copper binding site present at the amino terminus of the latter albumins. Affinities of all three proteins for zinc were similar, suggesting that the albumin amino terminus is not the primary zinc ion binding site.     

A Review of: “RECEPTOR BIOCHEMISTRY AEiD METHODOLOGY,J.C. Venter & L.C. Harrison,Eds. Alan R. Liss,New York, 1964, hardbound; Vol.1: 238 pages, $46.00; V01.2: 306 pages, $52.00; Vo1.3: 184 pages, $34.00”

Abstract

Prothrombin complex (P.C.) preparations obtained by batch adsorption onto DEAE-Sephadex are highly enriched in C4. Based on this observation a technique has been elaborated where the P.C. analogue is further submitted to precipitation by ethanol and batch adsorption of impurities on DEAE-Cellulose. Unaltered C4 is obtained in a 2 days process with a yield corresponding to 40 % of the starting material (cryoconcentrate supernatant).