148 REPORT — 1887. 



close together that it is not possible to separate them by fractional heat- 

 coagulation. The separation is effected as follows : the sodium sulphate 

 extract is saturated with magnesium sulphate ; this precipitates the 

 globulins, leaving the albumins in solution. Magnesium sulphate also 

 causes the swelling-up of the proteid numbered 6 in the foregoing enu- 

 meration of the proteids of tymph-cells ; but on complete saturation 

 with this salt, the swollen-up lumps become somewhat shrunken, and 

 can be removed by filtration with the globulins. The jjrecipitate on 

 the filter is then washed with saturated solution of magnesium sulphate 

 until the washings do not give the proteid reactions, and distilled water 

 is then added to the filter. The salt adhering to the globulins enables 

 them to dissolve in the water, while the jelly-like proteid remains un- 

 dissolved. In this solution of globulins the a variety can be removed by 

 heating to 50° and filtering, the second globulin remaining in solution. 

 This second globulin, for which I should propose the name cell-globulin 

 fi, resembles serum-globulin in all its properties. It coagulates at 75° 0., 

 is precipitated by dialysis, is also precipitated completely by saturation 

 with maguesium sulphate, and incompletely by saturation with sodium 

 chloride. That white blood-corpuscles are a source of serum-globulin 

 was first pointed out by A. Schmidt,' who showed that on their disinte- 

 gration in shed blood, two of the products resulting are paraglobulinand 

 fibrin ferment. The name paraglobulin is now almost abandoned ; the 

 term serum globulin is hardly applicable to a proteid existing in lymph- 

 cells ; hence it seems necessary to multiply terms and provisionally to 

 designate this globulin by a new name. 



3. The alhumin ivhich coagulates at 73° C. — This is present in small 

 amount, being, on heating to 78°, often not more than a cloudiness in 

 the liquid from which the globulins have been removed by saturation 

 with magnesium sulphate and filtration. In those cases in which a larger 

 amount than this was present, it was found to be identical in its properties 

 with sernm-albvimin. It has been found, however, that the serum, 

 albumin of warm-blooded animals can by fractional heat-coagulation be 

 separated into a, /3, and y varieties coagulating respectively at 73°, 77°, 

 and 83° C.^ This albumin of lymph-cells is therefore identical with 

 serum-albumin a ; but, for the reasons just specified, it seems advisable 

 here again to introduce a new term and provisionally to speak of this 

 proteid as cell-albumin a. 



4. The alhumin which coagulates at 80° 0. — This is, except for the dif- 

 ference in a iew degrees of its heat-coagulation temperature, identical 

 with seram-albumin y. It is present in exceedingly minute quantities, 

 and is often altogether absent. It may bo named, in symmetry with the 

 other proteids, cell-albumin /?. 



5. Alhumoses and Peptone. — After filtering off all the foregoing 

 proteids which are precipitable by heat, a certain amount of proteid 

 material still remains in solution. This is not the jDCCuliar mucinoid 

 proteid to which allusion has already been made. That is carried down 

 by and removed with the heat coagulum, as will be fully explained in the 

 next section : but this proteid residue consists of albumoses, the j| name 

 given by Kiilme and Chittenden to those substances which are inter- 

 mediate between ordinary proteids, and peptones. The amount of 

 albumose, or perhaps proteose would be a better name, varies consider- 



' Schmidt, Pfliiger's Archiv, vol. vi. p. 445. 



- Halliburton, ' Proteids of Serum,' Jown. of Physiology, 1885. 



