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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
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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