I 



x TABLE OF CONTENTS 



CHAPTER V 



PAGE 



SALTS OF ALBUMIN AND ACIDS 55 



Older methods of determining the extent of combination of 

 albumin and acids. Electrometric procedure. Researches 

 of Bugarsky and Liebermann, Manabe and Matula. Relation 

 between concentration of protein and of acid to the extent 

 of combination. Viscosity of acid albumin. Parallelism of 

 ionisation and viscosity ; precipitation by alcohol ; depres- 

 sion of the freezing point. Combination of albumin with 

 different acids. Optical rotation of the albumin salts. 

 Optical behaviour in various acids. The acid-albumin of Adolf 

 and Spiegel. Precipitation of albumin by acids. 



CHAPTER VI 

 SALTS OF ALBUMIN AND ACIDS (continued) .... 80 



Hydrolysis of albumin salts. Determination of mean degree 

 of hydrolysis and of mean basic dissociation constant of 

 albumin. Role of the terminal amino-groups and of the 

 imino-group of the peptide linkage. Properties of desamino- 

 glutin and of acid-albumin. Combination of albumoses and 

 peptone with acids. 



CHAPTER VII 

 SALTS OF ALBUMIN AND BASES ...... 93 



Electrometric measurement of the combination of albumin 

 with bases. Classification of combination with various strong 

 bases according to their dissociation constants. Parallelism 

 of viscosity, precipitation by alcohol, and ionisation of albu- 

 minates. Precipitation of albumin by concentrated alkalis. 

 Alkali caseinates. Equivalent conductivity of sodium, potas- 

 sium and ammonium caseinates. Detection of normal ionisa- 

 tion into metal ions. Determination of degree of dissociation 

 and of mobility of caseinate ions. Valency of caseinate ions 

 ascertained from the conductivity curve. Electrometric 

 determination of the combination of casein and alkali. 

 Existence of a casein-saturated complex and of a simple 

 caseinate, both with a trivalent casein ion. Molecular weight 

 of casein. 



CHAPTER VIII 

 ALTERATIONS IN STATE OF THE ALKALI PROTEINS WITH LAPSE 



OF TIME .no 



Alterations with time exhibited by viscosity, electrical con- 

 ductivity, and extent of combination in the alkali proteins. 

 Explanation on the basis of a rearrangement of the peptide 

 linkage from the lactam to the lactim form. Relation to other 

 rearrangements. Optical rotation of the alkali proteins. 



