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Àâòîðèçàöèÿ |
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Ïîèñê ïî óêàçàòåëÿì |
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Rosenberg I.M. — Protein Analysis and Purification |
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Ïðåäìåòíûé óêàçàòåëü |
Lipid modification, phosphatidylinositol specific phospholipase 255—256
Lowry method 110 114—115
Lymphocytes, solubilization of 108
Lyophilization 121
Lysis 33—34
Maltose binding protein (MBP) fusion proteins 347
Mammalian cells, foreign proteins in 353—354
Mass spectrometry 208
Membrane proteins 135—151
Membrane proteins, adsorbers 294—296
Membrane proteins, butanol extraction 140—141
Membrane proteins, detergents 141—151
Membrane proteins, fractionation of 254
Membrane proteins, integral 139—141
Membrane proteins, isolation of 138—139
Membrane proteins, peripheral 136—138
Membrane proteins, phosphorylation of 227
Membrane proteins, protein cleavage and 187—188
Membrane proteins, supports for 153—182
Membrane proteins, target protein detection 170—180
Metabolic labeling of cells 226—227
Metabolic labeling with mevalonic acid derivitives 249—250
Metabolic labeling, experiment protocols for 22—24
Metabolic labeling, GPI structure and 256
Metal chelate chromatography 319
Methylation 257
Mevalonic acid derivatives 249—250
Micelle molecular weight 144—145
Microsequencing 183—204
Microsequencing, partial proteolysis 200—201
Microsequencing, protein hydrolysis and 200
Microsequencing, protein transfer and 198—199
Microsequencing, protocols of 196—198
Microsequencing, SDS-PAGE protocol 197—198
Microsequencing, theory of 201 203
Modified peptides 207—260
Modified proteins, degradation 258
Modified proteins, desialylation 220—222
Modified proteins, enzymatic prenylation 250—251
Modified proteins, glycosylation 208—224
Modified proteins, hydroxylation 257
Modified proteins, kinase and 230—232
Modified proteins, lipid modification 245—256
Modified proteins, lysine 257
Modified proteins, mass spectrometry and 208
Modified proteins, methylation 257
Modified proteins, N-glycanase 214—215 218—220
Modified proteins, N-glycosidase F 215—216
Modified proteins, N-linked oligosaccharide chains and 210
Modified proteins, nuclear magnetic resonance 208
Modified proteins, O-glycanase 218—220
Modified proteins, O-glycosidase 217—218
Modified proteins, O-glycosylation and 216—219
Modified proteins, phosphorylation 224—244
Modified proteins, potato acid phosphatase 228—229
Modified proteins, proline 257
Modified proteins, proteolytic processing and 259—260
Modified proteins, recombinant proteins 250—251
Modified proteins, sialylation and 220
Modified proteins, sugars and 211—212
Modified proteins, transamidation 257
Modified proteins, ubiquitination 258
Molecular weight cut-offs 76 121
Molecular weight determination 75—77
Monoclonal antibodies 35
N-chlorosuccinimide mapping 190—192
N-glycanase 214—215 218—220
N-glycosylation 213—216
N-Hydroxysuccinimide (NHS) 48
N-linked oligosaccharide chains 210
N-myristoylation 245—247
N-terminal amino acid 199—203
NC (nitrocellulose) membranes 187—188
Neuraminidase 219—222
Nitrocellulose, protein transfer to 154—156
Nitrogen decompression 104
Nondenaturing immunoprecipitation 40—41
Nonequilibrium pH gradient electrophoresis (NEPHGE) 88—90
Nonionic detergents 108 144—145
Nuclear extracts 106—108
Nuclear magnetic resonance 208
Nucleic acids 109
O-glycanase 218—220
O-glycosidase 217—218
O-glycosylation 216—219
o-iodosobenzoic acid 194
Ohm’s Law 64—65
Oligosaccharides, glycoproteins and 222
Oligosaccharides, removal from glycoprotein 214—215
Oligosaccharides, tunicamycin and 216
Optical density (OD) 109
Ornstein, L. 56
Page see "Polyacrylamide gel electrophoresis"
Palmitoylation 245—247
Partial proteolysis, microsequencing and 200—201
Particulate-associated proteins 135—151
Peptide mapping 183—204
Peptide mapping by proteolysis 186—187
Peptide mapping, chemical cleavage and 194—195
Peptide mapping, cysteine residues and 194—195
Peptide mapping, electrophoresis and 186—187
Peptide mapping, formic acid cleavage 193—194
Peptide mapping, N-chlorosuccinimide and 190—192
Peptide mapping, phosphopeptide mapping 234—239
Peptide mapping, protocols for 186—187
Peptide mapping, SDS-PAGE and 183—184
Perfusion chromatography 296
Periodic acid/Schiff method (PAS) 159—160
Pestle and tube homogenizers 104—105
Peterson, G. 114
pH measurement of gel slices 88—90
Phosphatidylinositol specific phospholipase C (PI-PLC) 255—256
Phosphoamino acid analysis 234—242 244
Phosphohistidine residues 242—244
Phosphopeptide mapping 234—239
Phosphopeptide mapping, one dimensional 234
Phosphopeptide mapping, preparation for 235
Phosphopeptide mapping, thin-layer chromatography and 237—239
Phosphopeptide mapping, two dimensional 234—235
Phosphorylation in SDS-gels 232—234
Phosphorylation of membrane proteins 227
Phosphorylation of substrates 232—234
Phosphorylation of target proteins 225—227
Phosphorylation, alkaline phosphatase and 229
Phosphorylation, enzymatic dephosphorylation 227—234
Phosphorylation, kinases and 230—232 233
Phosphorylation, modified proteins and 224—244
Phosphorylation, phosphoamino acid analysis 239—242
Phosphorylation, protocols of 225—227
PinPoint 348—349
Plasma membrane, nonionic detergents and 108
Polyacramide gels 68 77 192—193
Polyacramide gels, enzyme activity in 90—91
Polyacramide gels, protein band detection in 71—72
Polyacramide gels, protein cleavage and 184—185
Polyacrylamide gel electrophoresis (PAGE) 2 35—37 55—57
Polyclonal antibodies 34
Polyethylene glycol 128
Polypeptides 9 70
Polyvinylidene diflouride (PVDF), protein transfer to 154—156
Ponceau S 158—159
Postmitochondrial polypeptides 82
Potato acid phosphatase 228—229
Precipitation techniques, ammonium sulfate 124—125
Precipitation techniques, methanol chloroform 130
Precipitation techniques, polyethylene glycol and 128
Precipitation techniques, protocols for 124—132
Precipitation techniques, salting out 124—125
Precipitation techniques, selective denaturation 129—131
Precipitation techniques, trichloroacetic acid 130—131
| Proline 5 257
Protease 341
Protease, antiprotease cocktail 32—33
Protease, digestion 333—334
Protease, enzymes 91—92
Protease, inhibitors 92—93 102—103
Protease, localization of 91—92
Protease, proteolytic enzymes 91—92
Protein A 171 306—308
Protein bands, detection of 71—72
Protein bands, electroelution of 79—81
Protein bands, extraction of 77—78
Protein cleavage 184—189
Protein cleavage, cyanogen bromide 189—190
Protein cleavage, hydroxylamine cleavage 192—193
Protein cleavage, membrane and 187—188
Protein cleavage, NC membranes and 187—188
Protein cleavage, polyacrylamide gels and 184—185
Protein cleavage, proteotytic enzymes for 185
Protein cleavage, protocols 187—189
Protein cleavage, PVDF and 187—189
Protein concentration 109
Protein denaturation 129—131
Protein detection 153—182
Protein fractionation by HIC 298—299
Protein hydrolysis, microsequencing and 200
Protein identification, sucrose gradients 41—43 46
Protein immobilization 314—315
Protein purification 99—132
Protein purification with acetone 126—127
Protein purification, methodology 4
Protein purification, precipitation techniques 124—131
Protein purification, protocols 124—131
Protein purification, subcellular localization 110
Protein purification, ultrafiltration 120—121
Protein quantitation 110—111
Protein quantitation, acetone and 131
Protein quantitation, bicinchoninic acid method 110 115—116
Protein quantitation, Bradford method 110 111—114
Protein quantitation, flourescamine protein assay 117—118
Protein quantitation, Lowry method 110 114—115
Protein quantitation, UV absorption and 123
Protein recovery from dilute solutions 130
Protein recovery from dried gel 77—79
Protein recovery from the blot 160—161
Protein recovery, ammonium sulfate precipitation 119—120
Protein recovery, detergent based solvent system 162
Protein recovery, organic solvent system 161—162
Protein separation, isoelectric focusing and 84—86
Protein separation, low molecular weight proteins 69—71
Protein sequences 8 203—204
Protein structure 5—19
Protein structure, alpha helix 10—11
Protein structure, antiparallel pleated sheets 11—12
Protein structure, beta structure 11
Protein structure, chemical characteristics 14—17
Protein structure, consensus sequences 17—18
Protein structure, four levels of 6—14
Protein structure, hydrogen bonds 11 13
Protein structure, isoelectric point 15
Protein structure, primary structure 6—7
Protein structure, quaternary structure 13—14
Protein structure, secondary structure 10—12
Protein structure, tertiary structure 12—13
Protein synthesis in vitro translation and 330—331
Protein tracking 19—53
Protein transfer, colony/plaque lifts 157
Protein transfer, dot blots and 156—157
Protein transfer, protocols of 154—157
Protein transfer, to membrane supports 153—158
Protein transfer, to nitrocellulose 154—156
Protein transfer, to polyvinylidene diflouride 154—156
Protein ZZ 350
Protein-protein interactions 141
Protein-to-detergent ratio 149
Proteins 246—247 see "Target
Proteins in solution 117—124
Proteins, biotinylation of 172
Proteins, cross-linking of 50
Proteins, cysteine residues and 118—119
Proteins, dialysis 121—123
Proteins, disulfide linked 85
Proteins, eukaryotic 339—340
Proteins, frozen storage 118
Proteins, fusion 327 336—337
Proteins, isoprenylation 247—250
Proteins, lipid modification 246—256
Proteins, membrane 135—151
Proteins, microsequencing 198—199
Proteins, recombinant 250
Proteins, stabilization of 117—119
Proteins, storage of 117—119
Proteins, structure of 5—19
Proteins, transfer of 153—182
Proteoglycans 21 223—224
Proteolysis, limited 186—187
Proteolytic enzymes 91—92 132 185
Proteolytic processing 259—260
Pulse-chase protocol 24—25
PVDF blots, chemical cleavage and 189—195
PVDF membranes 187—189 199
PVDF membranes, kinases on 231—232
PVDF membranes, microsequencing and 196—198
R groups 5—6 13
Radioactive sugars 211
Radioactively labeled DNA 94
Radiolabeled lectin 167
Radiolabeled proteins 176
Recombinant gene products 337—339 342—346 350—352 355—361
Recombinant protein techniques 325—361
Recombinant protein techniques from yeast 350—352
Recombinant protein techniques, affinity tags 341—361
Recombinant protein techniques, antibody production 326—327
Recombinant protein techniques, baculoviral vectors 352—353
Recombinant protein techniques, DEAE-dextran chloroquine method 357—359
Recombinant protein techniques, DNA template 328—329
Recombinant protein techniques, E coli 335—361
Recombinant protein techniques, glycerol shock 356—357
Recombinant protein techniques, GST fusion protein purification 343—344
Recombinant protein techniques, GST fusion protein transformants analysis 342
Recombinant protein techniques, GST removal 344—345
Recombinant protein techniques, insect cells 352—353
Recombinant protein techniques, maltose binding protein 347
Recombinant protein techniques, protocols of 328—335
Recombinant protein techniques, transfections 357—360
Reducing agents 83
Reverse zymography 92—93
Reversible staining 74—75 158—159
S cerevisiae 352
S TagTM system 347—348
Salting out 124—125
SDS see "Sodium dodecylsulfate"
SDS-gels, phosphorylation in substrates in 232—234
SDS-PAGE 35—37 47—48 67 71 77 79—81 132 164 168 196 307
SDS-PAGE, molecular weight determination by 75—77
SDS-PAGE, peptide mapping and 183—184
SDS-PAGE, protocol alterations 197—198
SDS-polyacrylamide gels 57—58 232—234
Sepharose 4B 313—314
Sequential immunoprecipitation 39—40
Sialylation 220
Silver staining 73—74
Slide-A-Lyzer® Dialysis Cassettes 122—123
Sodium dodecylsulfate (SDS) 56—58 232—234
Solvent-induced autolysis 105
Stable transfections 359
Stacking gel, casting of 60—61
Staining techniques 72—75 158—160
Staphylococcal protein A 350
Staphylococcus aureus 36 39
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