A Review of: “Plasma Fibronectin (Structure and Function) J. McDonagh,Ed. Marcel Dekker,New York, 1985; hardbound, 269 pages, $59.75”

Abstract

Subcellular Components; Preparation and Fractionation G.D. Birnie, ed., 2nd edition, Butteworths, London and University Park Press, Baltimore, 1972; 320 pages, hardbound, $19.50

Methodological Developments in Biochemistry Volume 2 Preparative Techniques E. Reid, ed., Longman, London, 1973; 220 pages; soft cover; $9.50

Methodological Developments in Biochemistry Volume 3 Advances with Zonal Rotors E. Reid, ed., Longman, London, 1973; 273 pages; soft cover; $9.50     

A Review of: “Methods of Protein Separation,N. Catsirapoolas,ed. Plenum Press,New York, 1975; 281 pages; hardbound; $27.50”

Tryporaastogotes of three strains of Trypanosoma cruzi were isolated from the blood of infected mice employing lymphoprep for separation of the red blood cells and a column of DEAE cellulose for removal of white cells and platelets. An average recovery of 45 to 5 8 percent of actively motile, infective organisms, free of contaminating blood cells was obtained. Protein and carbohydrate assays of the separated organisms revealed significant differences between the Tulahuen, a reticulotropic strain, and the House 510 and House 11, two myotropic strains of this parasitic species. The present procedure should provide sufficient parasites for physiological and biochemical studies; it has also served to indicate particular strain characteristics which may aid in a taxonomic classification of these organisms.     

A Review of: “Gel Permeation Chromatography,Eds. K.H. Altgelt and L. Segal Marcel Dekker,Inc., New York 1971 xvii + 646 pages ill., hard cover $24.75”

A simple, rapid procedure for the purification of uricase from mammalian tissue is reported. The procedure is based on the precipitation of mammalian uricase under certain dialysis conditions, and on its low solubility near neutral pH. Exceptionally high yields of homogeneous enzyme are obtained.     

A Review of: “Biological Recognition and Assembly,D. S. Eisenberg,J. A. Lake and C. F. Fox,Eds. Alan R. Liss,New York, 1980; hardbound, 355 pages, $52.00”

Two MMP-7-ase isoenzymes were purified 100-fold from rat muscle extract to apparent homogeneity, with an overall yield of 10%, using homogenization, ultracentrifugation, high-performance aqueous size-exclusion and high-performance anion exchange chromatography methods. When using a TSK G-2000SW column, the separation resulted in a 6-fold purification and 30% recovery of isoenzymes B and C. This concentrated enzyme extract was then passed through a TSK-DEAE-2SW column, using salt gradient at pH 7.5, with an additional 25-fold purification and 90% recovery of the isoenzymes. Two symmetrical enzyme peaks, representing isoenzymes B and C, were detected when performing purity tests of the active enzymes on the anion exchanger and reversed-phase HFLC columns. The procedures involved are extraction, ultracentri-fugation, chromatographies and enzyme assays and require less than five hours.     

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).