364 BEPOET— 1888. 



of the proteids present. Cell-globalin a and the two albumins, especially 

 the /3 variety, are present in only small quantities, and cell-albumin fi 

 seems to be often altogether absent. 



Some further investigations upon the properties of the mucin-like 

 proteid have led me to conclude that it belongs to a class of proteids 

 called by Hammarsten ' nucleo-albumins. These proteids resemble 

 globulins in the way in which they are precipitated by salts, and also in 

 their insolubility in distilled water. They, however, differ from globulins 

 by yielding an ash rich in phosphorus, and on gastric digestion yielding 

 an insoluble residue of the nature of nuclein, which is also rich in phos- 

 phorus. The substance was purified in the following way : — 



An extract of the cells in 10 per cent, sodium chloride solution has a 

 slimy mucus-like consistency ; it filters very slowly, but it can be 

 separated from the insoluble residues of the cells (nuclei, &c.) by filtra- 

 tion under pressure. On pouring this filtrate into a large excess of dis- 

 tilled water, the globulins are precipitated in a finely flocculent condition, 

 and sink to the bottom ; whereas the mucin-like proteid is precipitated 

 throughout the water in the form of cohesive strings, which in a few 

 minutes contract, and finally collect in sticky lumps which float upon the 

 surface of the water. These were thoroughly washed with and kneaded in 

 distilled water, and finally washed with rectified spirit and absolute 

 alcohol. This substance after ignition yielded an ash rich in phosphorus. 

 It was easily soluble in 1 per cent, hydrochloric acid ; on diluting this 

 solution fivefold or even tenfold with water there was no reprecipitation 

 of the proteid. 



A large quantity of such a solution in 1 per cent, hydrochloric acid 

 was dilated till the strength of the acid was 0*2 per cent. On keeping 

 this solution at the temperature of 40° C. in an incubator for twenty-four 

 hours there was no precipitate ; but on adding to it an active solution of 

 pepsin there was in the course of three or four hours, at the same tempera- 

 ture, a cloudiness, which became denser, and ultimately a flocculent pre- 

 cipitate formed. This did not tend to disappear or become lessened after 

 very prolonged digestion ; it could not, therefore, be anti-albumid, the 

 comparatively insoluble by-product which occurs in the digestion of 

 ordinary albumin ; for anti-albumid is, after prolonged digestioiij largely 

 converted into peptones. 



This precipitate was collected, washed with 0'2 per cent, acid, and 

 then distilled water and alcohol. It was soluble in alkalis {e.g., baryta 

 water), and it also yielded an ash rich in phosphorus. 



The filtrate from which the precipitate bad been removed contained 

 albumoses and peptones, the usual products of gastric digestion, and con- 

 tained the merest traces of phosphorus. No such precipitate was pro- 

 duced by pancreatic digestion. 



It is on these results of gastric digestion, as well as on the other 

 physical and chemical characteristics of this substance, that I am inclined 

 to include this proteid among the nucleo-albumins. Similar mucin-like 

 globulins have been separated by Hammarsten from the cells of the sub- 

 maxillary gland, which contain, however, true mucin in addition ; from 

 the synovial fluid and from bile, whei-e they have long been mistaken for 

 mucin. 



With regard to the remaining proteids in lymph cells, I have not 



' Zeit. Physiol. Chem, vol. xii. p. 163. 



