Am'oc°tu,ri8^7arm'}  Proteids  of  Seeds  of  Abrus  Precatorius.  505 
was  then  dried  over  sulphuric  acid.  The  residue  was  in  dark  brown 
scales.    It  consisted  of  globulin  with  some  coloring  matter. 
It  is  not  possible  to  remove  all  the  globulin  by  dialysis,  so  the 
liquid,  after  dialyzing  for  seven  days,  was  filtered  into  rectified  spirit, 
which  precipitated  the  remaining  proteids.  After  standing  under  the 
alcohol  six  to  eight  weeks  the  globulin  was  coagulated,  and  the 
precipitate  was  collected,  dried,  and  treated  with  distilled  water,  which 
dissolved  out  a  proteid.  This  proteid  is  an  albumose.  The  chloride 
of  sodium  method  may  be  used  instead  of  the  ammonium  sulphate ; 
it  takes  a  longer  time,  but  gives  products  freer  from  coloring  matter. 
For  chemical  examination,  the  albumose  is  readily  prepared  by 
boiling  and  filtering  an  aqueous  infusion  of  the  seed.  The  globulin  is 
coagulated  while  the  albumose  remains  in  solution. 
Properties  of  the  globulin. — 1.  It  is  insoluble  in  distilled  water,  but 
readily  soluble  in  10  to  15  per  cent,  sodium  chloride  or  magnesium 
sulphate  solution ;  soluble  to  a  less  extent  in  5  per  cent,  sodium  chlo- 
ride solution,  and  scarcely  at  all  in  0'75  per  cent. 
2.  It  is  completely  precipitated  from  solution  by  saturation  with 
sodium  chloride  after  slightly  acidifying,  and  with  ammonium  sulphate, 
whether  the  solution  be  neutral,  acid,  or  alkaline. 
3.  It  is  coagulated  by  heat  in  10  per  cent,  magnesium  sulphate  so- 
lution, between  75°  and  80°  C,  the  liquid  being  made  distinctly  acid; 
in  10  per  cent,  sodium  chloride,  between  66°  and  73°  C. 
4.  When  the  solution  in  10  per  cent,  sodium  chloride  is  placed  in 
the  incubator  at  35°  to  40°  C,  and  allowed  to  remain  twenty-four  or 
even  forty-eight  hours,  no  precipitation  occurs ;  a  reaction  in  marked 
contrast  to  that  given  by  some  vegetable  globulins.  In  its  high 
coagulation  temperature,  and  in  its  non-precipitation  from  solution  by 
prolonged  exposure  to  a  moderate  heat,  abrus-globulin  agrees  with  the 
proteid  I  have  described  in  the  juice  of  the  fruit  of  Carica  papaya, 
which,  from  its  resemblance  to  serum-globulin,  I  have  called  vegetable 
paraglobulin.1  The  vegetable  myosins  occurring  in  the  cereals,  wheat, 
rye  and  barley,  have  a  lower  coagulation  temperature  than  the  para- 
globulins,  viz.,  50°-55°  C,  and  are  precipitated  from  solution  and 
rendered  insoluble  by  a  prolonged  exposure  to  a  temperature  of  35°- 
40°  C.2 
Properties  of  the  albumose. — 1 .  Soluble  in  cold  or  boiling  distilled 
1 "  Nature  of  Papain,  etc.,"  Jour,  of  Physiol.,  vol.  vi.,  p.  353. 
2  "  Physiol.  Soc.  Proc,"  February  12,  1887. 
