346 



INDEX 



Chymotrypsins, action on — cont. 

 chymotrypsinogen, 159-163 

 corticotropin, 310, 311 

 growth hormone, 318-319, 322, 



324, 326 

 melanotropin, 305, 334 

 ribonuclease, 212-213, 219 

 ribonuclease peptides, 214-216 

 serum albumin, 291 

 tobacco mosaic virus, 257-258, 

 268 

 dialysis rate, 108, 110 

 oxidized, enzymic hydrolysis of, 

 175 

 Chymotrypsinogen 

 action of chymotrypsin on, 159-163 

 action of leucinaminopeptidase on, 



164-168 

 activation, 155-167 

 amino-acid composition, 81 

 basic peptides from, 86-87, 175 

 cysteic acid peptides from, 84 

 dialysis rate, 108, 110 

 reaction with DFP, 177 

 Collagen 

 e-NHg groups, covalent linkage, 



221 

 viscosity, 38 

 Conalbumin 

 configuration, 55-56 

 physico-chemical properties, 55-56 

 viscosity, 38 

 Corticotropins 

 biological activity and structure, 



312-313, 335-337 

 enzymic hydrolysis, 310-312 

 partial synthesis, 312 

 periodate oxidation, 336 

 relation to melanotropins, 313, 



333-337 

 species differences, 73, 307-313 

 Counter current distribution, 257, 304, 



312,314 

 C-terminal groups, see Carboxyl 



groups 

 Cysteic acid peptides, isolation of, 



84-85, 186-187 

 Cytochrome C, 66-72 

 dialysis rate, 108, 110 

 haemopeptide from, 70 

 species differences in, 71 

 structure, 70-72 



Denaturation, AA, 45, 49-62, 233-238, 



250-254, 280, 339-340 

 Deuterium exchange in 

 insulin A chain, 32 

 jS-lactoglobulin, 32 

 poly-DL-alanine, 23-34 



kinetics of, 23-34 

 poly-DL-serine, 33 

 ribonuclease, oxidized, 32 

 triglycine, 30-31 

 Dialysis 

 rate of, and ionic strength, 112-113 

 andpH, 110 

 and temperature, 109 

 and urea, 110 

 separation of proteins, by, 104- 

 115,291 

 Diffusion coefficient, see under in- 

 dividual proteins, physico- 

 chemical properties of 

 Dinitrophenylation (see also Amino 

 terminal group determination) 

 microtechnique, 91 

 of proUne peptides, 264 

 Dinitrophenyl protein, from tobacco 

 mosaic virus, 267 

 enzymic degradation of, 268 

 removal of DNP residue from, 268 

 Disulphide bonds 

 and stabihty of proteins, 44, 45, 62 

 oxidation, 175, 211, 220, 224-232, 



236, 282-284, 316, 322 

 reductive cleavage, 224-232, 316 

 in ribonuclease, position of, 219- 

 221, 228-230 



Edman degradation, 215-218, 264- 

 266 



Electrophoresis in 

 agar, 241-243 



cellulose columns, 94-97, 291 

 multicompartment apparatus, 90 

 paper, 90, 141, 148-150, 227-229, 



232, 268, 305 

 starch gel, 140, 307-308, 316 



Electrostatic interaction in 

 haemoglobin, 44 

 polymethacrylic acid, 47-49 

 protein models, 39-41, 46 



Enolase, 338-340 



Esterification of proteins, 236, 330- 

 332 



