Ole Aalund

Gamma globulins of bovine lacteal secretions

Abstract Gamma globulin components of bovine colostrum and dry secretion were compared with their counterparts in serum by means of immunoelectrophoresis, anion exchange chromatography, and double-diffusion antigenic analysis. Although comparable components appeared immunochemically and physicochemically similar no matter where they originated, the proportional amount of each component varied greatly according to the character of the secretion. Thus, electrophoretically fast and slow 7S gamma globulin components were found to selectively accumulate in dry secretion relative to other serum proteins. Colostrum formation involved the same discrimination relative to other serum proteins and also a virtually complete discrimination against slow 7S gamma globulin in favor of a fast component. Bovine gamma-1M and gamma-1A globulins were found in lacteal secretions.

Isolation and characterization of ovine gamma globulins

Abstract Fractions of sheep serum were obtained by anion-exchange column chromatography on DEAE Sephadex, and gel filtration on Sephadex G-200 which contained only one of the following ovine gamma globulins: 7S gamma-2, 7S gamma-1, and gamma-1M. The gamma globulins were identified by immuno-electrophoresis, starch-gel electrophoresis, analytical ultracentrifugation, and by their content of antibody activity. By these physical criteria they were identical to their counterparts in human serum. Circumstantial evidence indicated that ovine serum also contains a protein analogous to the gamma-1A globulin of human serum.

Physical heterogeneity of bovine γ-globulins: Characterization of γM and γG globulins☆

Abstract The γG globulins of bovine serum were characterized by anion exchange chromatography, immunoelectrophoresis, zone electrophoresis, ultracentrifugation, and analysis of the products of papain digestion. Their properties were similar to those of analogous components of human serum. Fast and slow γG globulins were distinguished on the basis of differences in electrophoretic migration rates, chromatographic elution positions, and biological activities (complement fixation). Antigenic differences were detectable only in immunoelectrophoretic patterns (spur formation). Bovine γM was found to have properties quite similar to those of the analogous protein in human serum as determined by the methods of gel filtration, immunoelectrophoresis, anion exchange chromatography, ultracentrifugation, and reduction with mercaptoethanol. Bovine γA was provisionally recognized in immunoelectrophoretic analyses of serum and chromatographic fractions.

PHYSICAL HETEROGENEITY OF BOVINE GAMMA GLOBULINS: GAMMA-1M GLOBULIN ELECTROPHORETIC HETEROGENEITY.

Summary In the bovine species, gamma-1M globulin occurs as an electrophoretic continuum with most molecules of near mean mobility. No electrophoretic sub-groups of particularly high concentration, as described for 7S gamma globulins, were noted. Complement-fixing antibody activity was associated with bovine gamma-1M globulin molecules whose mean electrophoretic mobility was slower than the mean mobility of the protein as a whole. The marginal extent of this manifestation argues against anticipation of as heterogeneous a distribution of particular biological activities within the gamma-1M globulin spectrum as has been shown to be the case with 7S gamma globulins.

Isolation and characterization of ovine serum alkaline phosphatases

Summary The ovine serum alkaline phosphatase (orthophosphoric monoester phospho-hydrolase, EC 3.1.3.1) isozymes A, B, and C were fractionated by gel nitration on Sephadex G-zoo and by anion-exchange chromatography on DEAE-Sephadex. Alkaline phosphatase activity was confined to the middle peak of the Sephadex G-200 chromatogram. Sephadex G-200 had an exclusion value of 200 000, and it is concluded that the alkaline phosphatases have a molecular size not exceeding the average molecular size of molecules with molecular weight 200 000. The B-phosphatase was almost entirely confined to sera from sheep of blood group O. However, the majority (68.5 %) of blood-group O substance in O-serum was found in the first peak of the Sephadex G-200 chromatogram, whereas only 17.9% of this substance was found in the second peak. It is likely, that therefore, the alkaline phosphatase isozymes in serum do not exist in a complex with blood-group O substance. The K m′ values for p -nitrophenyl phosphate were found to be quite different for the A- and B-phosphatases. The PO 4 8− -inhibition was non-competitive, and the mechanism involved in this phenomenon is discussed; it is suggested that the inhibition might be due to reactivity at an allosteric site which would be consonant with the observation of non-competitive inhibition by phosphate in the presence of excess Mg 2+ . The L -phenylalanine inhibition was higher for O-serum than for R-serum, 70% and 56% inhibition respectively, suggesting an intestinal origin of the B-phosphatase. EDTA inhibited both O- and R-serum 100%. Some SO 4 2− -inhibition (non-competitive) was noted with both O- and R-sera.