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Index of Subjects 393 INDEX OF SUBJECTS Amino acids Double rdraction of flow, 218-227 Raman spectra of, 40-49 of myosin, 221 relation to keto acids, 32-39 of tobacco mosaic virus, 222-226 Amino group, ionization of, 44-46 Amphibian organizer, chemical nature of, 385-391 Electrical mobility Amphoteric behavior of amino acids, 24-26 and molecular radius, 236, 237 Amphoteric behavior of proteins, 24-31 of B. coli, 107 Antibodies of denatured egg albumin, 148 molecular weight of, 172, 173 of egg albumin, 228-231 surface fihns of, 188 of gelatin, 232, 233 Asymmetry of latex, 239, 240 of protein molecules, 118-120, 143, 144, 146, of pituitary hormones, 282-284 199-227 of prolactin, 106 of virus proteins, 349-351 of ragweed pollens, 238, 239 of serum proteins, 231,232, 339, 382 Bacterial polysaccharide, 98, 101, 102, 139 Electrically charged groups, 8-20 basic groups, 8, 9 Carboxyl group, ionization of, 41-44 carboxyl group, 9 Cephalin, neural induction by, 385-388 dissociation of, 11-13 Chitin, 97 phenolic hydroxyl, 9-11 Chromoproteins, 286-300 sulfhydryl, 9-11 reversible dissociation of, 294-296 Embryological development and purine content of Coagulation, 144-146 tissues, 105, 106 Comparative biochemistry of proteins, 79-90 Energy of activation, of hemoglobins, 83, 84 m denaturation, 138-141, 146, 147 of keratins, 79-83 of visual purple, 293, 299 of neurokeratins, 87, 88 Enzymes of neuroproteins, 83-87 prosthetic group and protein carrier, 286-300 of protamines, 79 yellow, 292, 293 of serum proteins, 83 Expansion patterns, 159, 175-178 Condroitinsulfuric acid, 93-95 Conjugated proteins, 151-153, 286-300 Fabric structure, 48, 49, 55, 56, 110, 120-139, 147, Contraction of muscle and denaturation of myo- 161, 181, I84-186 sin, 153-156 Frequency hypothesis of protein structure, 58-66, Cyclol, see Fabric structure 81, 109-111, 134, 135, 278, 279 Denaturation, 140-170, 375 Gastric polysaccharide, 98 by high frequency radiations, 163-170 Globulin from horse serum, 338, 339 chemical changes in, 150, 151 Glycoproteins, 91-102 energy of activation of, 138-141, 146, 147 Guanidine, structure of, 46 of myosin, 153-157 of pepsinogen, 318-324 Hemoglobin, structure of, 290-292 of virus proteins, 345-347 Heparin, 97 reversibility of, 151 Hormones, protein nature of, 262-274 Dielectric constants of peptides and proteins, 13- insulin, 264 20 parathormone, 264 and molecular shape, 201-206 pitocin, 281, 282 of dipolar ions, 15 pitressin, 281, 282 Dielectric behavior of zein, 210-213 prolactin, 262, 269, 271, 273, 274 Diffusion of prolamines, 209, 210 secretin, 264 Diffusion of proteins, 196-207 thyroglobulin, 264 Dipole moments, 13-23 Hyaluronic acid, 91-93 Dissociation constants of peptides and proteins, Hydrogen ion dissociation curves, effect of neutral 11-13, 21-23 salts on, 1-7 394 Immunological behavior and protein constitution, Prosthetic group and protein carrier, 286-300 369-374 Proteolytic enzymes and protein structure, 50-57 Immunological methods for identification of serum proteins, 376-384 Radiations, denaturation by, 163-170 Insulin, 275-285 Raman spectra of amino acids and peptides, 40-49 acetylation of, 267, 268, 272 Rotatory dispersion of gelatin, 246-249 amino acids in, 278 composition of, 264, 271 Salted out films, 183 reduction of, 265, 266, 280, 281 Serum protein fractions, 232, 241, 242, 254 sulfur in, 264-267, 276-279, 284, 285 immunochemical determination of, 376-384 Isoelectric point, definition of, 237, 238 phase rule study of, 331-340 Skeleton films, 183 Keto acids, relation to amino acids, 32-39 S-layers, 182, 183 Snake venoms, 238 Leaves, metabolism of proteins in, 67-78 Solubility of crystalline proteins, 301-317, 325-330 Light, effect on metabolism in leaves, 67-78 of cystine, 314, 315 of denatured protein, 150 Macromolecules, ultracentrifugal study of, 351-368 of virus protein, 317 Metabolism of proteins in green leaves, 67-78 Specificity of proteins, 127-129, 272 Monolayers and multilayers, 114-117, 129, 130, Structure of proteins 136, 137, 149, 171-189 and proteolytic enzymes, 50-57 at air-water interface, 190-195 chemistry of, 58-66 of antigens and antibodies, 188 Synthesis of peptides, 53-55 of denatured protein, 142, 143 of pepsin, 161-163, 183 Thymonucleic acid compounds, 112-114 structure of, 181, 182 Tissue proteins, composition of, 103-108 thickness of, 114-116, 149, 180, 181, 187, 188 Titration curves, 1-20, 24-31 viscosities of, 177, 178 effect of neutral salts on, 1-20 Mucoitinsulfuric acid, 95-97 of denatured protein, 141, 142 Mucosaccharides, 91-102 of enzymes, 238 Net charge of proteins, 233-236 Neural induction, 385-391 Ultracentrifugation of macromolecules, 361-368 Neutral salts, Ultrafiltration of proteins, 252-26i and optical activity of proteins and amino acids, 244-251 Virus proteins effect on hydrogen ion dissociation curves, 1-7 chemical nature of, 351-354, 359, 360 Nucleoproteins in tissues, 103-108 denaturation of, 345-347 hydrolysis by enzymes, 347 Optical rotation of gelatin, 244-251 immunological properties of, 348, 349 molecular homogeneity, 343-345 Patterson-Harker diagrams, see X-ray analysis properties of, 341-360 Pepsin purification of, 341-343 production from pepsinogen, 318-324 size and shape of particle, 349-351 solubility of, 301-317, 323 Viscosity Pepsinogen and molecular shape, 200-207 conversion into pepsin, 318-324 during reduction of insulin, 265 denaturation of, 318-320 of monolayers and multilayers, 177, 178 Periodicity hypothesis, see Frequency hypothesis Visual purple, 293, 294, 299 Pigments, prosthetic group and protein carrier, 286-300 X-ray analysis, 109-121 Precipitin reaction, 369-374 of multilayers, 114-116, 149 Prolactin as a protein, 262, 269, 271, 273, 274 of thymonucleie acid compounds, 112-114 Prolamines, physical chemistry of, 208-217 Patterson-Harker diagrams, 48, 49, 130-132 395 INDEX OF PARTICIPANTS Abramson, H. A., 189, 261 Kendall, F. E., 158, 159, 374, 375, 376-384 Andrews, D. H., 48 Kunitz, M., 325-330 Astbury, W. T., 17, 18, 47, 48, 56, 109-121, 134, Lackrnan, D. B., 102 137, 149, 156, 157, 158, 186, 193, 204, 205, Langmuir, I., 134, 135, 136, 159, 160-162, 163, 214, 216, 217, 226, 250, 251,272, 359, 364 171-189, 193-195, 226 Barth, L. G., 103-108, 385-391 Laufter, M., 226, 227 Bateman, J. B., 148 Loring, H. S., 56, 205, 206, 261,341-360 Bates, R. W., 271, 272, 285 Mathieu, M., 120, 170, 186, 225 Beale, H. P., 356, 357, 358 Mehl, J. W., 186, 204, 205, 207, 215, 216, 218-227 Bell, F. O., 109-121 Melin, M., 261 Bergrnann, M., 56, 57, 65 Meyer, K., 89, 91-102, 323, 366, 367 Blanchard, K. C., 39 Mirsky, A. E., 64, 146, 150-163 Block, R. J., 79-90 Moos, A., 339, 340, 375 Bull, H. B., 7, 31, 47, 48, 108, 120, 138, 140-149, Morgan, V., 282 163, 193, 215, 242, 260 Moyer, L. S., 7, 30, 31, 78, 107, 139, 148, 205, Carman, R. K., 1-7, 17, 251 206, 216, 228-243, 260, 283, 339, 375 Carpenter, D. C., 18, 23, 38, 244-251 Mudd, S., 90, 102, 118, 193, 272, 273, 316, 355, Cohn, E. J., 8-20, 23 357, 365 Danielli, J. F., 56, 64, 118, 147, 148, 149, 163, Myers, W. G., 56, 120 188, 190-195,242 Neurath, H., 23, 57, 65, 118, 120, 138, 147, 148, Davenport, C. B., 138, 355 160, 170, 185, 193, 196-207, 215, 216, 217, Davson, H., 251 226, 272, 316, 366, 367, 368, 375 de Tomasi, J. A., 77 Niemann, C., 58-66, 134-136, 137, 157, 158 du Vigneaud, V., 271, 275-286, 298, 299, 314, Northrop, J. H., 325-330 315, 364, 366 Oncley, J. L., 19, 21-23 Edsall, J. T., 7, 18, 40-49, 57, 249, 250 Riddle, O., 273 Farr, W. K., 139 Salomon, K., 298 Ferry, J. D., 21-23 Shack, J., 21-23 Fricke, H., 164-170 Stanley, W. M., 299, 300, 341-360, 365, 366, 367, Fruton, J. S., 38, 48, 50-57, 89, 119, 216, 217, 368 272, 283, 297, 298, 323, 366 Steiger, R. E., 134 Furchgott, R. F., 157, 187, 188, 330 Steinhardt, J., 89, 119, 120, 215, 216, 217, 272, Goldsmith, E., 390 284, 298, 299, 300, 301-317, 323, 324, 357, Gorin, M. H., 242 365 Grabar, P., 252-261 Stern, C., 358 Graft, S., 103-108, 385-391 Stern, K. G., I01, 119, 206, 271, 272, 273, 282, 283, 284, 286-300, 358, 365 Gudernatsch, F., 284 Tiselius, A., 241 Harris, M., 89, 120, 242, 272, 283, 284 Vickery, H. B., 67-78, 134, 137, 158, 260 Harrison, R. G., 390 Waddington, C. H., 65, 108, 119, 357, 389, 390 Heidelberger, M., 7, 107, 108, 136, 139, 260, 330, Watson, C. C., 208-217 339, 369-375, 383 White, A., 38, 56, 64, 65, 77, 78, 90, 119, 139, Herbst, R. M., 32-39 158, 242, 262-274, 283, 365, 366 Herriott, R. M., 89, 285, 316, 317, 318-324 Williams, J. W., 206, 208-217, 365, 367 Hisey, A., 298 Wrinch, D. M., 18, 19, 48, 49, 64, 65, 77, 78, Hitchcock, D. I., 6, 18, 19, 24-31, 251, 252 122-139, 147, 148, 157, 158, 184, 323, 324 Jameson, E., 315, 331-340, 383, 384 Wyckoff, R. W. G., 361-368 .
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