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Rosenberg I.M. — Protein Analysis and Purification
Rosenberg I.M. — Protein Analysis and Purification



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Íàçâàíèå: Protein Analysis and Purification

Àâòîð: Rosenberg I.M.

Àííîòàöèÿ:

This comprehensive, practical and user-friendly manual is designed to be a practical progression of experimental protocols that an inexperienced investigator may follow when embarking on a biochemical or biotechnology project.


ßçûê: en

Ðóáðèêà: Áèîëîãèÿ/

Ñòàòóñ ïðåäìåòíîãî óêàçàòåëÿ: Ãîòîâ óêàçàòåëü ñ íîìåðàìè ñòðàíèö

ed2k: ed2k stats

Ãîä èçäàíèÿ: 1996

Êîëè÷åñòâî ñòðàíèö: 434

Äîáàâëåíà â êàòàëîã: 07.05.2009

Îïåðàöèè: Ïîëîæèòü íà ïîëêó | Ñêîïèðîâàòü ññûëêó äëÿ ôîðóìà | Ñêîïèðîâàòü ID
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Ïðåäìåòíûé óêàçàòåëü
2-mercaptoethanol (2-ME)      83—84
Acrylamide concentration      59—60
Affinity chromatography      19 303—322
Affinity tags, recombinant proteins and      341—361
Alkali extraction      138—139
Alkaline phosphatase, phosphorylation and      229
Amino acids, bonds and      9—10
Amino acids, histidine purification      321
Amino acids, hydropathy values of      9
Amino acids, N-terminal      199—203
Amino acids, nonpolar      15
Amino acids, nonpolar R groups      13
Amino acids, phosphohistidine residues      242—244
Amino acids, R groups      5—6
Amino acids, sequence analysis      217
Anti-CRD      256
Antibodies      34
Antibodies, antigen-antibody method      153—154
Antibodies, biotinylating      179—180
Antibodies, coupling      306—308
Antibodies, immunoblots and      179—180
Antibodies, monoclonal      35
Antibodies, polyclonal      34
Antibodies, production of      326—327
Antibodies, purifying      179—180
Antibodies, techniques      35—37
Antibody coupling      306—308
Antigen-antibody method      153—154
Antiparallel pleated sheets      11—12
Antiprotease cocktail      32—33
Autographa califomica      352
Autophosphorylation      233
Autoradiography      71—72 177—178 180
Bacillus sub tills      138
bacteria      139 169
Bacteria, purifying proteins from      101—102
Baculoviral vectors      352—353
Bead mill homogenizers      103
Bicinchoninic acid (BCA) method      110 115—116
Bioactivity, retention of      21
BioRad Mini Protean II      64
Biotin      28—29 171
Biotinylation of proteins      172
Biotinylation, domain-selective      29—31
Blotting methods      158—160
Blotting methods, blocking      163—164
Blotting methods, primary antibody and      163—164
Blotting methods, southwestern analysis      169—170
Bovine uroplakin, CNBr cleavage of      191
Bradford method      109 111—114
Bradford spot test      278
Buchner funnel      106
Butanol extraction      140—141
Carbohydrate analysis      222—223
Cell disruption      102—105
Cell extracts      32 101—109
Cell labeling      21—24 226—227
Cellulose films      68
Centrifuge speeds      3
Chemical cleavage      189—195
Chemical cross-linking      46—53
Chloramine T method      22 31—38
Chloroform/methanol extraction      21
Chromatofocusing      292—293
Chromatography      265—322
Chromatography, affinity      303—319
Chromatography, chromatofocusing      292—293
Chromatography, gel filtration      267—280
Chromatography, high performance liquid      2 266 279—283 294 300—303
Chromatography, HPLC-ion exchange      294
Chromatography, hydrophobic interaction chromatography      296—303
Chromatography, hydroxylapatite      321—322
Chromatography, ion exchange      283—293
Chromatography, lectin affinity      317—319
Chromatography, ligand affinity      312—313
Chromatography, membrane adsorbers      294—296
Chromatography, metal chelate      319—320
Chromatography, perfusion      296
Chromatography, reversed phase HPLC      300—303
Chromatography, terminology used in      266—267
Colorimetric detection      173—174
Consensus sequences, protein structure      17—18
Copolymerized substrate      93—94
Covalent modification      207—260
Critical micelle concentration (CMC)      142—144
Cross-linking      46—53
Cuatrecasas      312
Cysteine residues      81 194—195
Database searches      203—204
Davis, B.      56
Dayhuff, T.      70
DEAE-dextran      357—358
DEAE-dextran chloroquine method      358—359
Denaturation      91 99—132 136
Desialylation      220—221
Detergents      141—151
Detergents, choosing      146—147
Detergents, classification of      145
Detergents, critical micelle concentration      142—144
Detergents, gel filtration      146
Detergents, hydrophile-lipophile balance      145
Detergents, ionic      149—150
Detergents, nonionic      144—145 150
Detergents, nucleic acids and      109
Detergents, protein recovery and      162
Detergents, protein-to-detergent ratio      149
Detergents, protocols of      147—149
Detergents, removal of      149—150
Detergents, solubilization      146 148—149
Diagonal gels      84—85
Dialysis      121—123
Differential centrifugation      106
Dimethylpimelimidate      306—307
Direct autoradiography      177
Disulfide bond formation      83—85 119
Dithiobis      51—52
Dithiothreitol (DTT)      83—84
DMSO shock      356—357
DNA, cDNA      4 16 20
DNA, DNA-binding proteins      94—95 169
DNA, eukaryotic systems      354—355
DNA, probes      169
DNA, protein sequences and      8
DNA, radioactively labeled      94
DNA, replication of      353
DNA, template preparation      328—329
DNA, transfection of      355—356
Dot blots      156—157
Edman reagent      201—203
Electrophoresis      55—97 186—187 237—238
Electrophoresis, attaching gel cassette      62—64
Electrophoresis, BioRad Mini Protean II      64
Electrophoresis, buffer composition      236
Electrophoresis, comb removal      63
Electrophoresis, Coomassie blue staining      62
Electrophoresis, electrophoresis chamber      80
Electrophoresis, gel drying      68
Electrophoresis, gel staining      72—73
Electrophoresis, gradient gels and      66—67
Electrophoresis, nonreducing      52
Electrophoresis, postmitochondrial polypeptides      82
Electrophoresis, preparing the sample      61—62
Electrophoresis, safety considerations      71
Electrophoresis, two-dimensional gel systems      81
ELISA (enzyme linked immunosorbent assay)      35 161
Elutrap™      77 79—81
Endoglycosidase H analysis      219 334—335
Enhanced chemiluminescence      175—176
Enzymatic activity, staining for      91
Enzymatic cleavage      184—189
Enzymatic dephosphoryltaion, protocols for      227—234
Enzymatic detection methods, target protein detection      172—173
Enzymatic prenylation      250—251
Enzymes      91—92 118 see
Enzymes, glutathione-S-transferase (GST) fusion proteins      341
Enzymes, kinases      224—225 230—233
Enzymes, lactoperoxidase      26
Enzymes, N-glycanase      214—215 218—220
Enzymes, neuraminidase      219—222
Enzymes, potato acid phosphatase      228—229
Epitope mapping      165
Eukaryotic proteins, purification of      339—340
Eukaryotic proteins, transfection-expression and      354—355
Exchanger matrix      286
Extracti-Gel® D      150—151
Fasman, G.      325
Fast atom bombardment mass spectrometry (FAB-MS)      213
FLAG biosystem      346—347
Flourescamine protein assay      117—118
Fluorography      178—179
Formic acid cleavage      193—194
Fusion proteins      327 336—337
Fusion proteins, glutathione-S-transferase      341
Fusion proteins, maltose binding protein (MBP)      347
Fusion proteins, removing the GST      344—345
Fusion proteins, solubilization of      339
Gabriel, O.      91
Gel bonding, agarose in      81
Gel cassette, attaching to the apparatus      62—64
Gel filtration chromatography      267—280
Gel filtration chromatography, application-loading      275
Gel filtration chromatography, Bradford spot test      278
Gel filtration chromatography, buffers      123
Gel filtration chromatography, choice of buffer      270
Gel filtration chromatography, column size      270—271
Gel filtration chromatography, detergents      146
Gel filtration chromatography, equipment      269
Gel filtration chromatography, flow rate      273
Gel filtration chromatography, gel-degassing      271—272
Gel filtration chromatography, hydrostatic pressure      273—275
Gel filtration chromatography, molecular weight determination      276
Gel filtration chromatography, packing the column      272—273
Gel filtration chromatography, spin columns in      277—278
Gel reactions, post-electrophoresis and      93—94
Gersten, D.      91
Glutathione-S-transferase (GST) fusion proteins      341
Glycerol shock      356—357
Glycopeptide sequencing      203
Glycoproteins      21
Glycoproteins in glycosylation      215—216
Glycoproteins, binding of      317—318
Glycoproteins, elution of      319
Glycoproteins, oligosaccharide removal from      214—215
Glycoproteins, oligosaccharides and      222
Glycoproteins, purification of      319
Glycoproteins, sialylation of      220
Glycoproteins, staining of      159—160
Glycoproteins, tunicamycin and      216
Glycosaminoglycans      21
Glycosidase inhibitors      211
Glycosyl phosphatidylinositol      252—253
Glycosylation      208—224
Glycosylation, endoplasmic reticulum and      209
Glycosylation, glycoproteins and      215—216
Glycosylation, golgi apparatus      209
Glycosylation, immunoprecipitates and      215—216
Glycosylation, N-glycosylation      213—216
Glycosylation, oligosaccharide removal      214—215
Glycosylation, proteoglycans and      223—224
Glycosylation, protocols for      213—224
Glypiation      251—253
GPI structure      256
Gradient gels      66—67
Green, N.      349
GST fusion proteins, purification of      342—344
Guanidine hydrochloride      91 138
Hemagglutinin      349—350
High performance liquid chromatography (HPLC)      2 266 279—283
High performance liquid chromatography (HPLC), column designs      280—281
High performance liquid chromatography (HPLC), helpful tips      281—282
High performance liquid chromatography (HPLC), HPLC-ion exchange chromatography      294
High performance liquid chromatography (HPLC), packing materials      280
High performance liquid chromatography (HPLC), reversed phase      300—303
High performance liquid chromatography (HPLC), size exclusion      282—283
High pressure homogenizers      103—104
Histidine purification      321
Holzman, L.      338
HPLC      see "High performance liquid chromatography"
Hydrogen bonds      11 13
Hydropathy scale      15
Hydrophile-lipophile balance      145
Hydrophobic interaction chromatography (HIC)      296—303
Hydrophobic sites      15—16
Hydroxylamine cleavage      192—193
Hydroxylapatite chromatography      321—322
Hydroxylation      257
Immunoaffinity matrices      310—311
Immunoaffinity purification      305—306
Immunoblotting      164—165 179—180
Immunodetection      170—180
Immunoprecipitation      35—36 215—216
Immunoprecipitation, nondenaturing      40—41
Immunoprecipitation, principles of      34—37
Immunoprecipitation, protocol for      37—39
Immunoprecipitation, sequential      39—40
In vitro transcription      327—328 329—330
In vitro translation      328—328 330—332
Indirect autoradiography      178
IODO-GEN® method      27
Ion exchange chromatography      283 286
Ion exchange chromatography, batch adsorption      288
Ion exchange chromatography, buffers in      287
Ion exchange chromatography, chromatofocusing      292—293
Ion exchange chromatography, exchanger matrix      285—286
Ion exchange chromatography, functional groups      284—285
Ion exchange chromatography, ion exchange column      289—290
Ion exchange chromatography, protocols for      288 291—293
Ion exchange chromatography, regeneration of sephadex exchangers      291
Ion exchange chromatography, regeneration of sepharose ion exchangers      292
Ion exchange chromatography, starting pH      288—289
Ion exchange chromatography, theory of      283—284
Ionic detergents      145 149—150
Isoelectric focusing (IEF)      84—88
Isoelectric point      15 84 284
Isoprenylation      247—250
Kessler, S.      36
Kinases      224—225 230—233
Labeling of cells      21—24
Labeling of protein      21—22
Labeling, Chloramine T method      22 31—38
Labeling, metabolic      22—24 226—227 249—250
Labeling, radioactive sugars      211
Labeling, surface proteins      25—29
Lactoperoxidase      26
lacZ fusion proteins      336—337
Laminin binding      166
Lectin affinity chromatography      317—319
Lectin binding      165 167—169
Lectin, radiolabeled      167
Lectins, carbohydrate analysis and      222—223
Ligand affinity chromatography      312—313
Ligand binding, protocols of      165—167
Ligand blotting      164—165
Ligand interaction      49—50
Linderstrom-Lang, K.      6
Linear gradient gels      66—67
Lipid bilayer      141
Lipid modification      245—256
Lipid modification, glypiation      251—253
Lipid modification, isoprenylation      247—250
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