A Review of: “Progress in Separation and Purification Vol. 3, E. S. Perry and C. J,van Oss,eds., Willy/Intersciencc,New York, 1970; xi + 316 pares; hard cover; 515.95”

The optimal culture conditions of exopolysaccharides (EPS) production in submerged culture medium by Pleurotus geesteranus 5 ^# were determined using an orthogonal matrix method. The optimal defined medium (per liter) was 60.0 g maltose, 5.0 g tryptone, 1 mM NaCl, 5 mM KH₂PO₄, and initial pH 6.0 at 28 °C. In the optimal culture medium, the maximum EPS production was 16.97 g/L in a shake flask. Two groups of EPSs (designated as Fr-I and Fr-II) were obtained from the culture filtrates by size exclusion chromatography (SEC), and their molecular characteristics were examined by a multiangle laser-light scattering (MALLS) and refractive index (RI) detector system. The approximate weight-average molar masses of the Fr-I and Fr-II of EPS were determined to be 3.263 × 10⁴ and 5.738 × 10³ g/mol, respectively. The low values of polydispersity ratio (1.176 and 1.124 for Fr-I and Fr-II, respectively) of EPSs mean that these EPS molecules exist much less dispersed in aqueous solution without forming large aggregates. Furthermore, the experiments in vitro indicated that P. geesteranus 5^# EPS exhibit high antitumor and antioxidative effects.     

A Review of: “Biochemistry and Methodology of Lipids,Eds. A.R. Johnson and J.B. Davenport Wiley-Interscience,New York, 1971 x + 578 pages,ill., hard cover; $29.50”

A previous communication from this laboratory¹ as well as one from another³ described the separation of α₂-macroglobulin from swine serum. The products from both laboratories contained, in addition to α₂-macroglob-ulin, an additional macroglobulin contaminant with α₂-globulln mobility. Due to their physicochemical similarity these macroglobulins are not resolved using conventional column procedures such as ion exchange chromatography and gel filtration. Subsequent experiments have shown that immunoelectro-phoretically pure swine α₂-macroglobulln is present, in good yield (65%) in the breakthrough effluent of columns of Bio-Gel A-1.5m-Reactive Blue 2 while the contaminating macroglobulin is tightly bound. The production of highly purified swine α₂-macroglobulin utilizing this observation is the subject of the present report. The product of the separation was found to be homogeneous when subjected to Immunoelectrophoresis, at a concentration of 14–16 mg/ml, and diffused against antiswlne whole serum antibody. The production of monospecific antibody, a more stringent test for homogeneity, resulted when the purified α₂-macroglobulin was injected into rabbits. Physicochemical analyses on the purified product showed that swine and human α₂-macro-globulins are true homologs.