ARNOLD H! ^^^ERTH AND MARGARET BELLOWS 



675 



bination with gelati- "^-^ations, and this must have required a different 

 mechanism. We '•■ anot exclude the possibility that the primary- 

 cause of union between bacteria and protein is non-electrical (per- 

 haps a surface tension phenomenon), and that electrical neutraliza- 

 tion is a secondary effect which may or may not occur. 



Flocculalion with Crystallized Egg Albumin. 



Crystallized egg albumin was obtained by the method of Hopkins 

 and Pinkus (1898); this was dialyzed to remove the ammonium 

 sulfate. Experiments were conducted in buffer mixtures only 

 (Table III). 



TABLE III. 



Bacterium coli Suspension with Egg Albumin. 

 1 .0 cc. buffer mixture + 0.5 cc. albumin solution + 0.5 cc. coli suspension. 



Temperature = 40°C. X = agglutination within 1 hour. + = agglutination 

 within 4 hours. 



Agglutination of this strain of Bacterium coli did not occur at pH 4.8, 

 the isoelectric point of the albumin. A second strain of this organism 

 was agglutinated at pH 4.7 by an albumin concentration of 1 : 150. 



Flocculalion with Protalbumose and Heteroalbmnose. 



These albumoses were prepared from Witte's peptone by the 

 method of Pick (1898). The heteroalbumoses gave a clear solution 

 when boiled and adjusted to pH 7.0; the protalbumose required no 

 adjustment to give a clear solution. 



The protalbumose was completely soluble at all reactions tested. 

 The heteroalbumose, in a concentration of 1:400, was turbid at reac- 



