Action of Ox-blood serum upon Sea-urchin Eggs. 63 



to that of the other proteins investigated. On the other hand the 

 C0 2 - or " insoluble " globulin of serum, when isolated and dis- 

 solved in sea water, is no less potent than other proteins in in- 

 hibiting membrane-formation. A 0.3 per cent, solution of the 

 " insoluble " serum globulin very noticeably inhibits membrane- 

 formation, and yet a 3.7 per cent, solution of the mixed proteins 

 of serum, containing 0.33 per cent, of the C02-globulin, under the 

 conditions enumerated above only inhibits membrane-formation 

 to a barely perceptible extent. These facts would appear to lend 

 confirmation to the view advanced by Hardy 1 and myself 2 that 

 the various proteins in sera are not present therein in the free 

 condition, but bound together in a molecular complex. 



44 (653) 



Preliminary note. — The action of various agents upon the 

 secretion of milk. 



By ISAAC OTT, M.D., and JOHN 0. SCOTT, M.D. 



In these experiments we used the lactating goat, obtaining 

 the milk by aspiration with a water bottle. We found, as Macken- 

 zie has noted, an increased secretion from venous injections of 

 extracts of the mammary gland. The boiled gland was also active. 

 The pineal body, corpus luteum, and infundibulin were active 

 after a previous dose of atropin. Atropin and antipyrin greatly 

 decreased the secretion. Pilocarpin and digitalin augmented the 

 secretion. Pilocarpin in large doses was active after a preliminary 

 dose of atropin. Albumoses, peptones, and glucose increased the 

 secretion. Sodium, potassium and calcium chloride increased the 

 secretion. Eserine, muscarine, and nicotine did not augment the 

 secretion. 1/1000 of a drop of infundibulin increased the flow of 

 milk, and 1/100 of a drop caused a marked increase. Infundibulin 

 is a 20 per cent, extract of the infundibular part of the pituitary 

 body. 



1 W. B. Hardy, Journ. of Physiol., 33, 251, 1905 (Appendix). 

 4 T. Brailsford Robertson, Univ. of Calif. Publ. Physiol., 4, 25, 1911; "Die 

 physikalische Chemie der Proteine," Dresden, 1912, pp. 126-133. 



