Purification and properties of buffalo serum albumin

Based on a detailed study of the solubility of serum albumin, a procedure for its purification by selective ammonium sulphate precipitation has been developed. Using buffalo serum, first extraneous proteins were precipitated by making the serum 2.26 M saturated with ammonium sulphate at pH 7.0 and then albumin was precipitated from the supernatant at 1.9 M ammonium sulphate concentration at pH 4.2. The overall yield of serum albumin thus isolated was about 55% with a purity of 97%. The protein preparation gave a single nearly symmetrical peak on Sephadex G-100 column and virtually a single band on polyacrylamide gel electrophoresis in the presence and absence of SDS. Buffalo serum albumin has a molecular weight of 69,000 Da. The hydrodynamic properties such as Stoke's radius (3.70 nm), diffusion coefficient (6.03 X 10(-7) cm2/s) and frictional ratio (1.36) obtained by analytical gel chromatography, bilirubin binding characteristics and its interaction with anti-bovine serum albumin antiserum suggest that buffalo serum albumin is very similar to BSA in its molecular properties.     

Changes in the immunochemical properties of highly purified properdin in human serum.

The fate of highly purified properdin (P) upon introduction into normal human serum or properdin-depleted serum (RP) was investigated. It was observed that, concomitant with the activation of the alternate pathway components, properdin underwent immunochemical alterations characterized by a shift in mobility from gamma2 to beta2 position and by an increase in the sedimentation rate from 5.1S to between 6.8 and 9.3S. The immunoelectrophoretic behavior of C3 was also altered with the appearance of a beta2 arc in addition to the beta1C arc. The immunochemical properties of altered P resemble those of "native" properdin in fresh serum. The principle in serum (designated factor F) mediating these changes is a euglobulin with an approximate sedimentation rate and molecular weight of 9.0S and 250,000 daltons, respectively. The alteration in the immunochemical properties of P may be due to aggregation of P molecules or a complex formation between P and a serum euglobulin (probably C3) mediated by factor F and it is associated with loss of ability of P in initiate the alternate pathway of complement activation upon interaction with serum.     

Some observations on the dielectric properties of hemoglobin's suspending medium inside human erythrocytes.

Dielectric permittivity and conductivity data for human erythrocytes exhibit two consecutive dispersions with frequency in the range from 0.1 to 250 MHz. The dispersion observed above 50 MHz yields a circle in the complex impedance plane with its center on the real axis, suggesting a Debye relaxation, for the erythrocyte interior medium, centered in the microwave frequency range as for bulk water. Moreover, the Maxwell mixture equation, indicates that this "free" water forms most of the suspending medium of hemoglobin macromolecules. These results extend to lower frequencies (earlier results obtained by Schwan) with biological tissues such as muscles, skin, or liver at microwaves frequencies.     

Some ultrastructural observations on the microfilaria of Breinlia sergenti--nervous system

The amphids, cephalic papillae, phasmids, excretory complex, anal vesicle, rectal cells, G cell and the nerve ring are described in the microfilaria of Breinlia sergenti. The significance of these various structures in playing a nervous role in this organism is discussed, and a working hypothesis presented to explain the nervous co-ordination in this parasitic stage.