43Q 
Protcids  of  Maize. 
J  Am.  Jour.  Pharm. 
1         Aug,  1892. 
tendency  to  separate  in  spheroidal  form  from  sodium  chloride  solu- 
tions. It  may,  therefore,  be  extracted  without  the  aid  of  heat 
coagulation  from  the  crude  proteid  matter,  prepared  in  the  manner 
previously  described,  or  from  the  meal  remaining  after  the  extrac- 
tion of  the  myosin.  The  proteid  matter,  for  example,  is  dissolved 
in  5  per  cent,  aqueous  sodium  chloride,  and  the  vitellin  is  first 
precipitated  by  dilution  with  a  large  bulk  of  water,  then 
redissolved  by  heating  the  whole  to  45°,  and  finally  caused  to 
separate  in  spheroidal  form  by  cooling  the  solution  slowly  to  8°. 
The  crude  product  thus  obtained  may  be  purified  and  caused  to 
aggregate  into  larger  spheroids  by  repeating  the  treatment.  Maize 
meal  from  which  the  myosin  has  been  previously  extracted  by  cold 
water  may  be  treated  with  10  per  cent,  aqueous  sodium  chloride, 
the  crude  vitellin  precipitated  by  saturating  the  solution  with 
ammonium  sulphate,  and  purified  by  a  somewhat  long  process 
which  comprises  dissolving  the  crude  product  in  sodium  chloride 
solution,  reprecipitating  it  by  dialysis,  dissolving  it  again  in  salt 
solution,  heating  the  solution  to  separate  coagulable  impurities, 
precipitating  the  now  nearly  pure  product  with  acetic  acid,  redis- 
solving  the  precipitate  in  sodium  chloride  solution,  and,  finally  pre- 
cipitating the  pure  vitellin  by  dialysis. 
The  third  globulin,  which  is  characterized  by  its  solubility  in 
dilute  solutions  of  salts  other  than  chlorides,  and  its  insolubility  in 
water,  is  obtained  by  long-continued  dialysis  of  the  solutions  from 
which  the  other  globulins  have  already  separated.  It  was  not 
observed  in  the  preliminary  experiments,  owing  to  the  slow  rate  at 
which  ammonium  sulphate  and  the  alkaline  phosphates  diffuse. 
This  globulin  has  the  composition:  C,  52-38;  H,  6-82;  N,  15-21;  S, 
1-26,  and  is  thus  distinct  from  the  myosin  and  vitellin.  It  is 
further  distinguished  from  these  globulins  by  the  low  temperature, 
620,  at  which  it  is  completely  coagulated. 
Various  other  substances  isolated  during  the  investigation  were 
probably  formed  from  the  solutions  by  the  incidental  treatment, 
and  do  not  exist  as  such  in  maize. 
A  substance,  for  instance,  soluble  in  water,  not  coagulated  by 
heat,  and  in  general  behavior  resembling  the  proteoses,  was  left 
in  solution  in  the  dialyser  after  the  removal  of  the  myosin  and 
vitellin  in  the  differentiation  experiments  first  described.  It  did  not 
exist  in  the  original  proteid  substance,  since  the  latter  did  not  yield 
