Abstract
Bacterial hemagglutinin from Pseudomonas aeruginosa has been partially purified via a sequence of steps involving: removal of nucleic acids by streptomycin sulfate, precipitation of other proteins by heating to 70°C and acidification, fractionation by ammonium sulfate, dialysis and another heating. The partially purified preparations was found to agglutinate human leukocytes and thrombocytes in addition to its erythrocyte-agglutinating activity. The bacterial hemagglutinin was found to resemble phytohemagglutinins in its relative resistance to heating, to acid and to proteolytic enzymes. It resembles them also in metal requirement and in the kinetics of its adsorption to erythrocytes and its elution from them. Preliminary estimation indicates that the bacterial hemaglutinin is a protein (or a glycoprotein) of a molecular weight significantly smaller than that of Phaseolus phytohemagglutinin (of Phaseolus vulgaris). The bacterial hemagglutinin was not found to induce lymphocyte transformation at conditions suitable for the lymphocyte transformation induced by Phaseolus phytohemagglutinin, nor was it found to abolish such a transformation.
| Original language | English |
|---|---|
| Pages (from-to) | 165-173 |
| Number of pages | 9 |
| Journal | Biochimica et Biophysica Acta - General Subjects |
| Volume | 273 |
| Issue number | 1 |
| DOIs | |
| State | Published - 26 Jun 1972 |
Bibliographical note
Funding Information:This work was supported by a research grant No. 161-81-o6-6 of the Research Committee of Bar-Ilan University. The author thanks Miss Lea Mizrahi for her technical assistance.
Funding
This work was supported by a research grant No. 161-81-o6-6 of the Research Committee of Bar-Ilan University. The author thanks Miss Lea Mizrahi for her technical assistance.
| Funders | Funder number |
|---|---|
| Research Committee of Bar-Ilan University |