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1997-12-20
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1áLipoprotein(a) - Bindeglied zwischen Fettstoffwechsel undíGerinnungssystem ?óúñ1991ÑPetersª01.02.1995º121(49)¿1813 1818⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´†¶©®™
2áShielding affinity chromatographyíóúñ1994ÑPetersª01.02.1995º12¿1086 1086⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´†¶©®™
3á"One pot" protein purification by process integrationíóúñ1994ÑPetersª01.02.1995º12¿1087 1089⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´†¶©®™
4áLarge scale, in situ isolation of periplasmic IGF-I from E. coliíóúñ1994ÑPetersª01.02.1995º12¿1113 1117⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´†¶©®™
5áAn Interleukin-4-induced transcription factor: IL-4 Statíóúñ1994ÑPetersª01.02.1995º265¿1701 1706⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´†¶©®™
6áJak-STAT pathways and transcriptional activation in response toíIFNs and other extracellular signaling proteinsóúñ1994ÑPetersª01.02.1995º264¿1415 1421⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´†¶©®™
7áConstruction and characterization of a set of E. coli strainsídeficient in all known loci affecting the proteolytic stabilityóof secreted recombinant proteinsúñ1994ÑPetersª01.02.1995º12¿1107 1110⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´†¶©®™
8áWirkungsweise von Interferoneníóúñ1994ÑPetersª01.02.1995º7¿78 85⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´†¶©®™
9áRecent developments in heterologous protein production iníEscherichia colióúñ1994ÑPetersª01.02.1995º12¿456 463⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´†¶©®™
10áImproving secretion of recombinant proteins from yeast andímammalian cells: rational or empirical design ?óúñ1994ÑPetersª01.02.1995º432-434¿⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´†¶©®™
11áElectroelution of antigens immobilized on antibody-linkedíaffinity matricesóúñ1989ÑPetersª01.02.1995º177¿314 317⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´†¶©®™
12áCytokine antagonists and their potential therapeutic useíóúñ1994ÑPetersª01.02.1995º15(10)¿455 458⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´†¶©®™
13áMetal chelate affinity chromatographyíóúñ1978ÑPetersª02.02.1995º¿⌐Affinity Chromatography¬½Turkova, J¼Elsevier Sci.Pub.Comp.¡Amsterdam, Oxford, New York«12»147 150ãõØøœŒÀÃÕ¨´†¶©®™
14áMetal chelate affinity chromatography of hamster interferoníóúñ1978ÑPetersª02.02.1995º58¿149 152⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´†¶©®™
15áThe production, purification, and bioactivity of recombinantíbovine trophoblast protein-1 (bovine trophoblast interferon)óúñ1990ÑPetersª02.02.1995º4(10)¿1506 1514⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´Inclusion bodies; Renaturation; Stability; Purification;†Activity measurements¶©®™
16áPurification of human fibroblast interferon by zinc chelateíaffinity chromatographyóúñ1977ÑPetersª02.02.1995º252(17)¿5934 5935⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´†¶©®™
17áImmunoregulatory effects of ovine trophoblastin protein (oTP):íall five isoforms suppress PHA-induced lymphocyte proliferationóúñ1991ÑPetersª02.02.1995º19¿237 249⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´†¶©®™
18áBiotechnology product validation, part 3: chromatographyícleaning validationóúñ1994ÑPetersª02.02.1995º4¿22 28⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´†¶©®™
19áIntrauterine infusion of highly enriched bovine trophoblastíprotein-1 complex exerts an antiluteolytic effect to extendócorpus luteum lifespan in cyclic cattleúñ1989ÑPetersª09.10.1994º87(1)¿89 101⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´ESTRUS/*drug effects; LUTEOLYTIC AGENTS/*antagonists &†inhibitors; PREGNANCY PROTEINS/administration & dosage/isolation¶& purification /*pharmacology; ANIMAL ; AUTORADIOGRAPHY ; CATTLE©; ELECTROPHORESIS, GEL, TWO-DIMENSIONAL ; FEMALE ;®™
20áHeterologous gene expression and protein secretion from Candidaíglabrataóúñ1994ÑPetersª02.02.1995º19¿265 269⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´†¶©®™
21áRegulating biotechnology licensed productsíóúñ1989ÑPetersª02.02.1995º43(3)¿139 141⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´†¶©®™
22áHigh cell density fermentations for the production ofírecombinant proteins in E. coli with inducible systemsóúñ1993ÑPetersª02.02.1995º¿⌐Report of second PIBE workshop Integrating Biological Techniques ¬for Bioprocessing½Enfors, SO; Veide, A¼¡Sitges«»248 253ãõØøœŒÀÃÕ¨´†¶©®™
23áCharacterization of recombinant proteins: biochemical andíbiophysical criteria for the identity of native and renaturedóhuman tissue plasminogen activator and its mutantsúñ1994ÑPetersª02.02.1995º20¿1 22⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´†¶©®™
24áA model system for the continuous production of a heterologousíprotein using a novel secretion promoting factor which operatesóin Escherichia coliúñ1994ÑPetersª02.02.1995º37¿33 37⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´†¶©®™
25áAffinitätschromatographie an immobilisierten Metallioneníóúñ1989ÑPetersª02.02.1995º6¿2 4⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´†¶©®™
26áAffinity thermoprecipitation of lactate dehydrogenase andípyruvate kinase from porcine muscle using Eudragit boundóCibracron blueúñ1994ÑPetersª02.02.1995º37¿23 31⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´†¶©®™
27áGlycosylation of recombinant proteins: problems and prospectsíóúñ1994ÑPetersª02.02.1995º16(5)¿354 364⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´†¶©®™
28áEnzymatische Racematspaltung von Arylalkanolamineníóúñ1994ÑPetersª02.02.1995º12¿1340 1340⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´†¶©®™
29áBiotransformations in organic synthesisíóúñ1989ÑPetersª02.02.1995º¿⌐Modern Synthetic Methods¬½Scheffold, R¼Springer¡Berlin, Heidelberg«5»1 114ãõØøœŒÀÃÕ¨´†¶©®™
30áEffect of toluene-permeabilization on oxidation of D-Sorbitol toíL-Sorbose by Gluconobacter suboxydans cells immobilized inócalcium alginateúñ1994ÑPetersª02.02.1995º16(4)¿345 348⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´†¶©®™
31áBiotransformations catalyzed by the genus Rhodococcusíóúñ1994ÑPetersª02.02.1995º14(1)¿29 73⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´†¶©®™
32áProcess for the stereoselective biotransformation of acetoaceticíacid esters using yeastsóúñ1990ÑPetersª02.02.1995º3¿37 50⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´†¶©®™
33áBiocatalysis in reverse self-assembling structures: Reverseímicelles and reverse vesiclesóúñ1994ÑPetersª02.02.1995º16(5)¿409 415⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´†¶©®™
34áLymphokine receptors as therapeuticsíóúñ1989ÑPetersª03.02.1995º7(7)¿668 669⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´†¶©®™
35áInterleukin futuresíóúñ1989ÑPetersª03.02.1995º7(7)¿661 667⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´†¶©®™
36áDry enzyme-polymer complexes: stable organosoluble biocatalystsífor nonaqueous enzymologyóúñ1994ÑPetersª03.02.1995º16(2)¿175 178⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´†¶©®™
37áEnzymatic membrane bioreactors and their applicationsíóúñ1994ÑPetersª03.02.1995º16¿738 750⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´†¶©®™
38áChemical desinfection of chromatographic resins, part 1:ípreliminary studies and microbial kinetics.óúñ1994ÑPetersª03.02.1995º7(5)¿46 56⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´†¶©®™
39áChemical sanitization in process chromatography, part 2: in situítreatment of packed columns and long-term stability of resinsóúñ1994ÑPetersª03.02.1995º7(8)¿37 42⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´†¶©®™
40áPurification of human interleukin-4 from a secreted Escherichiaícoli mutantóúñ1991ÑPetersª03.02.1995º¿⌐PCT/US91/00006 (4th January 1991 filing date)¬½¼Schering Corp. (applicant)¡«»1 21ãõØøœŒÀÃÕ¨´Secretory E. coli system; Zn-IMAC, P-buffer pH 7.2, 1 M NaCl,†then buffer + 10% glycerol, elution at pH 5; cation exchanger;¶concentration to 20 mg/ml; GPC in citrate buffer pH 4.5©®™
41áHuman interleukin-4 muteinsíóúñ1988ÑPetersª03.02.1995º¿⌐PCT/US87/03114 (4th December 1987 filing date)¬½¼Immunex Corp.¡«»1 35ãõØøœŒÀÃÕ¨´Batch adsorption to S-Sepharose FF pH 3.6 50 mM ß-alanine, wash†with ß-alanine pH 4; elution with 50 mM HEPES pH 7.4 o.5 M NaCl;¶RP-4, acetonitrile-gradient, 2% rate; Mono-S, 50 mM Tris, pH 7.4;©elution in Tris, 100 mM, pH 8 + 1 M NaCl;®™
42áPurification of human interleukin-4 from a CHO-cell line cultureímediumóúñ1991ÑPetersª03.02.1995º¿⌐Patent number 5,034,133 (23th July 1991 filing date)¬½¼Schering Corp.¡«»1 12ãõØøœŒÀÃÕ¨´S-Sepharose FF pH 7.2, 13-15 mS/cm; elution at pH 7.2, 0.26 M†NaCl; S-Sepharose FF (small column) with gradient elution 0.12-¶0.5 M NaCl, pH 7.2; Zn-IMAC, pH 7.2 45-50 mS/cm, 0.5 M NaCl;©wash with Na-P-buffer pH 7.2, 0.5 M NaCl; elution at pH 6 in the®same buffer; GPC on Sephacryl S-200/100 HR Citrate, pH 4.5™
43áRecombinant proteins can be isolated from E. coli cells byírepeated cycles of freezing and thawingóúñ1994ÑPetersª14.02.1995º12¿1357 1360⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´†¶©®™
44áSchiff base copper (II) chelate as a tool for intermolecularícross-linking and immobilization of proteinóúñ1989ÑPetersª14.02.1995º161(1)¿52 58⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´†¶©®™
45áIsolation and characterization of miroplasminogeníóúñ1988ÑPetersª14.02.1995º263(32)¿1707117075⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´†¶©®™
46áPlasminogen: purification from human plasma by affinityíchromatographyóúñ1970ÑPetersª14.02.1995º170¿1095 1096⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´†¶©®™
47áThe glucose transporter of E. coli. Assignment of the 1H, 13Cíand 15N resonances and identification of the secondary structureóof the soluble IIb domainúñ1994ÑPetersª01.03.1995º219¿945 952⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´†¶©®™
48áSulfitolysisíóúñ1967ÑPetersª01.03.1995º¿⌐Methods in Enzymology¬½Hirs, CHW¼Academic Press¡New York, San Francisco, London«XI»206 208ã22õØøœŒÀÃÕ¨´†¶©®™
49áThe modification of cystine - cleavage of disulfide bondsíóúñ1984ÑPetersª01.03.1995º¿⌐Chemical reagents for protein modification¬½¼CRC Press¡Boca Raton, Florida«1»95 98ã7õØøœŒÀÃÕ¨´†¶©®™
50áStructural heterogeneity of the cytoplasmic and outer membranesíof Escherichia colióúñ1977ÑPetersª15.03.1995º471(1)¿92 104⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´CELL MEMBRANE/*ultrastructure; ESCHERICHIA COLI/*ultrastructure;†RIAL PROTEINS/analysis; CELL FRACTIONATION ; CENTRIFUGATION,¶DENSITY GRADIENT ; FREEZE FRACTURING ;©LIPOPOLYSACCHARIDES/analysis; MEMBRANE LIPIDS/analysis; MEMBRANE®™
51áNature of the regions involved in the insertion of newlyísynthesized protein into the outer membrane of Escherichia colióúñ1979ÑPetersª15.03.1995º553(2)¿224 34⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´CELL MEMBRANE/*metabolism/ultrastructure; MEMBRANE†PROTEINS/*biosynthesis; BACTERIAL PROTEINS/biosynthesis;¶ESCHERICHIA COLI ; MEMBRANE FLUIDITY©®™
52áInsertion of newly synthesized proteins into the outer membraneíof Escherichia colióúñ1978ÑPetersª15.03.1995º512(2)¿365 76⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´BACTERIAL PROTEINS/biosynthesis/*metabolism; ESCHERICHIA†COLI/*metabolism; MEMBRANE PROTEINS/biosynthesis/*metabolism;¶CELL FRACTIONATION ; CELL MEMBRANE/drug effects/metabolism;©CHLORAMPHENICOL/pharmacology; KINETICS ; METHIONINE/metabolism®™
53áDistribution of newly synthesized lipoprotein over the outerímembrane and the peptidoglycan sacculus of an Escherichia coliólac-lpp strainúñ1987ÑPetersª15.03.1995º169(12)¿5434 44⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´BACTERIAL OUTER MEMBRANE PROTEINS/*analysis/biosynthesis;†ESCHERICHIA COLI/analysis/growth &¶development/genetics/*metabolism;©LIPOPROTEINS/*analysis/biosynthesis; PEPTIDOGLYCAN/*analysis;®™
54áRelease of outer membrane fragments from normally growingíEscherichia colióúñ1976ÑPetersª15.03.1995º455(3)¿889 99⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´CELL MEMBRANE/*metabolism/ultrastructure; ESCHERICHIA†COLI/*metabolism/ultrastructure; BACTERIAL PROTEINS/metabolism;¶CELL DIVISION ; CELL FRACTIONATION ; FATTY ACIDS/metabolism;©LIPOPOLYSACCHARIDES/metabolism; MEMBRANE LIPIDS/metabolism;®™
55áA highly efficient procedure for the quantitative formation ofíintact and viable lysozyme spheroplasts from Escherichia colióúñ1987ÑPetersª15.03.1995º164(2)¿320 30⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´ESCHERICHIA COLI/*drug effects/ultrastructure;†MURAMIDASE/*pharmacology; SPHEROPLASTS/*drug¶effects/ultrastructure; BACTERIOLOGICAL TECHNIQUES ; CATIONS,©DIVALENT ; CELL WALL/drug effects; EDETIC ACID/pharmacology;®™
56áRelease of outer membrane fragments from wild-type Escherichiaícoli and from several E. coli lipopolysaccharide mutants by EDTAóand heat shock treatmentsúñ1989ÑPetersª15.03.1995º171(10)¿5262 7⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´BACTERIAL OUTER MEMBRANE PROTEINS/*metabolism; EDETIC†ACID/*pharmacology; ESCHERICHIA COLI/drug¶effects/*genetics/metabolism/ultrastructure; HEAT/*;©LIPOPOLYSACCHARIDES/genetics/*metabolism; CELL®™
57áPreferential release of new outer membrane fragments byíexponentially growing Escherichia colióúñ1978ÑPetersª15.03.1995º508(2)¿287 95⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´ESCHERICHIA COLI/cytology/growth & development/*metabolism;†MEMBRANE PROTEINS/biosynthesis/*metabolism; BACTERIAL¶INS/biosynthesis/metabolism; CELL MEMBRANE/metabolism; CELL-©FREE SYSTEM ; CYTOPLASM/metabolism; DIFFUSION®™
58áOuter-membrane vesicles released by normally growing Escherichiaícoli contain very little lipoproteinóúñ1981ÑPetersª15.03.1995º116(2)¿331 5⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´CELL MEMBRANE/*analysis; ESCHERICHIA COLI/*growth & development;†LIPOPROTEINS/*analysis; MEMBRANE PROTEINS/*analysis;¶ELECTROPHORESIS, POLYACRYLAMIDE GEL ; MOLECULAR WEIGHT ;©SUBCELLULAR FRACTIONS/analysis; SUPPORT, NON-U.S. GOV'T®™
59áThe effect of osmotic shock on the accessibility of the mureinílayer of exponentially growing Escherichia coli to lysozymeóúñ1978ÑPetersª15.03.1995º508(2)¿296 305⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´ESCHERICHIA COLI/*/growth & development; MURAMIDASE/*metabolism;†PEPTIDOGLYCAN/*metabolism; BACTERIOLYSIS ; CELL WALL ; KINETICS¶; OSMOTIC PRESSURE ; SPECIES SPECIFICITY ; SPHEROPLASTS©®™
60áAn efficient and reproducible procedure for the formation ofíspheroplasts from variously grown Escherichia colióúñ1976ÑPetersª15.03.1995º74(1)¿160 70⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´ESCHERICHIA COLI/*ultrastructure; SPHEROPLASTS/*ultrastructure;†CELL DIVISION ; CELL FRACTIONATION/methods; CELL¶MEMBRANE/ultrastructure; FREEZE ETCHING ; MICROSCOPY, ELECTRON ;©MURAMIDASE ; SPECIES SPECIFICITY®™
61áHow does lysozyme penetrate through the bacterial outer membrane?íóúñ1976ÑPetersª15.03.1995º443(3)¿534 44⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´CELL MEMBRANE/drug effects/*metabolism; ESCHERICHIA COLI/drug†effects/*metabolism; MURAMIDASE/*metabolism; BIOLOGICAL¶TRANSPORT ; CELL DIVISION ; EDETIC ACID/pharmacology; KINETICS ;©MAGNESIUM/pharmacology; MODELS, BIOLOGICAL ; OSMOTIC PRESSURE ;®™
62áHeterologous Protein Production In Yeastíóúñ1992ÑPetersª16.03.1995º62(1-2)¿79 93⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´†¶©®™
63áNatural human interferon-alpha 2 is O-glycosylatedíóúñ1991ÑPetersª21.03.1995º276( Pt 2)¿511 8⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´INTERFERON TYPE I/*chemistry/isolation & purification; AMINO†ACID SEQUENCE ; ANTIBODIES, MONOCLONAL ; CHROMATOGRAPHY,¶AFFINITY ; CHROMATOGRAPHY, HIGH PRESSURE LIQUID ;©ELECTROPHORESIS, POLYACRYLAMIDE GEL ; ENZYME-LINKED®™
64áSeparation of human leukocyte interferon components byíconcanavalin A agarose affinity chromatography and theirócharacterizationúñ1980ÑPetersª21.03.1995º0¿597 598⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´†¶©®™
65áCharacterization of the alpha subunit of the IFN-alpha receptor.íEvidence of N- and O-linked glycosylation and association withóother surface proteinsúñ1993ÑPetersª21.03.1995º150(8 Pt 1)¿3382 8⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´INTERFERON-ALPHA/*metabolism; MEMBRANE PROTEINS/*metabolism;†RECEPTORS, INTERFERON/*chemistry/metabolism; BINDING SITES ;¶GLYCOSYLATION ; HUMAN ; MOLECULAR WEIGHT ; PRECIPITIN TESTS ;©SUPPORT, NON-U.S. GOV'T ; SUPPORT, U.S. GOV'T, P.H.S. ; TUMOR®™
66áExpression of human interferon-alpha 2 in Sf9 cells.íCharacterization of O-linked glycosylation and proteinóheterogeneitiesúñ1993ÑPetersª21.03.1995º217(3)¿921 7⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´INTERFERON-ALPHA/*genetics/isolation & purification/metabolism;†AMINO ACID SEQUENCE ; ANIMAL ; BACULOVIRIDAE/genetics; BASE¶SEQUENCE ; CARBOHYDRATE SEQUENCE ; CARBOHYDRATES/analysis; CELL©LINE ; CHROMATOGRAPHY, HIGH PRESSURE LIQUID ; CLONING, MOLECULAR®™
67áCharacterization of interferon-alpha binding sites on human cellílinesóúñ1988ÑPetersª21.03.1995º8(6)¿803 11⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´INTERFERONS/*metabolism; RECEPTORS, IMMUNOLOGIC/*analysis;†AFFINITY LABELS/pharmacology; COMPARATIVE STUDY ; DETERGENTS ;¶GLYCOSIDE HYDROLASES/pharmacology; HUMAN ; POLYETHYLENE GLYCOLS©; SUPPORT, NON-U.S. GOV'T ; SUPPORT, U.S. GOV'T, P.H.S. ;®™
68áExpression of human interferon alpha H, an interferon with twoípotential asparagine-linked glycosylation sitesóúñ1987ÑPetersª21.03.1995º1(3)¿103 8⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´ASPARAGINE/*; GENE EXPRESSION REGULATION/*; INTERFERON ALFA,†BINANT/*genetics; BASE SEQUENCE ; CHROMOSOME DELETION ; DNA,¶BACTERIAL/isolation & purification; ESCHERICHIA COLI/genetics;©GENETIC VECTORS ; GLYCOSYLATION ; HUMAN ;®™
69áRecombinant human insulin-like growth factor II expressed iníEscherichia colióúñ1987ÑPetersª12.06.1995º5¿1047 1051⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´Sulfitolyse; Cystein zum Entschützen des Proteins (Entfernung†der SO3-Gruppen) im 2-fachen molaren Überschuß über S-SO3-¶Gruppen;©®™
70áCosolvent assisted protein refoldingíóúñ1990ÑPetersª12.06.1995º8¿1274 1278⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´Kenntnis des Faltungsweges ist essentiell für das Design eines†effizienten Faltungsprotokolls (!); PEG 1000-8000; Carbonic¶anhydrase B (CAB); 3-30 g/l©®™
71áRenaturation of recombinant proteins produced as inclusion bodiesíóúñ1994ÑPetersª12.06.1995º12¿89 101⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´Disulfide-Shuffling faster at basic pH (8-10); IB-purification;†solubilization; renaturation; Interleukin; ¶©®™
72áEffective renaturation of reduced lysozyme by gentle removal ofíureaóúñ1995ÑPetersª12.06.1995º8(2)¿201 205⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´Lysozym-Renaturierung; Diafiltration mit Dialyseschläuchen; 5†mg/ml Proteinkonzentration; >80% Faltungsausbeute (!)¶©®™
73áProtein folding intermediates and inclusion body formationíóúñ1989ÑPetersª12.06.1995º7¿690 697⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´†¶©®™
74áPolyethylene glycol enhanced protein refoldingíóúñ1992ÑPetersª12.06.1995º10¿1013 1019⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´†¶©®™
75áThe purification of eukaryotic polypeptides synthesized iníEscherichia colióúñ1986ÑPetersª12.06.1995º240¿1 12⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´Intracellular expression; Secreted proteins; Cytokines as†examples¶©®™
76áProtein foldingíóúñ1990ÑPetersª12.06.1995º270¿1 16⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´Aprotinin; BPTI; Refolding; Pathways†¶©®™
77áFolding proteinsíóúñ1989ÑPetersª12.06.1995º¿⌐Protein Structure: A practical approach¬½Jaenicke, R¼IRL Press¡Oxford«»191 223ãõØøœŒÀÃÕ¨´†¶©®™
78áProtein solubility, protein modifications and protein foldingíóúñ1985ÑPetersª12.06.1995º3¿298 306⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´Immobilisierung von Trypsin/Trypsinogen an CNBr-Sepharose;†trägergebundene Renaturierung; Chemische Modifikationen inkl.¶Auswirkungen auf die Renaturierungsausbeute©®™
79áProduction and secretion of protein by Streptomycetesíóúñ1995ÑPetersª12.06.1995º15(1)¿13 39⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´†¶©®™
80áA method for increasing the yield of properly folded recombinantífusion proteins: Single-chain immunotoxins from renaturation ofóbacterial inclusion bodiesúñ1992ÑPetersª12.06.1995º205¿263 270⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´L-Arginin-Zusazt zum Renaturierungspuffer; Step-by Step Zusatz†von Proteinlösung zum Renaturierungspuffer zur Erhöhung der¶Proteinausbeute/ml©®™
81áEfficient renaturation and fibrinolytic properties ofíprourokinase and a deletion mutant expressed in Escherichia colióas inclusion bodiesúñ1991ÑPetersª12.06.1995º195¿691 697⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´Verdünnung in 2.5 M Harnstoff, pH 8.8 (Tris-Puffer), 5 mM EDTA,†3 mM EtSH, T=15 C; Proteinkonzentration 0.2 mg/ml¶©®™
82áRefolding of recombinant Pneumocystis carinii dihydrofolateíreductase and characterization of the enzymeóúñ1993ÑPetersª12.06.1995º4¿16 23⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´PEG 1450 (0.5%) im Renaturierungpuffer; pH 7, 2 mM DTT, 2 mM†EDTA, Phosphat-Puffer; Proteinkonzentration 0.2 mg/ml; Dialyse¶gegen Puffer ohne Guanidin-HCl©®™
83áSingle-step purification and structural characterization ofíhuman interleukin-6 produced in Escherichia coli from T7 RNAópolymerase expression vectorúñ1991ÑPetersª12.06.1995º198¿541 547⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´0.4 mg/ml Proteinkonzentration; 10% Glycerin; Tris pH 8.0; 1†Schritt: Dialyse gegen 1 M Guanidin; 2 Schritt: Dialyse gegen¶Puffer; 2 mM/0.2 mM Glutathion (red/ox) als Redoxpaar©®™
84áThiol exchange catalysed refolding of small proteins utilizingísolid-phase supportsóúñ1988ÑPetersª13.06.1995º31¿21 28⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´Isoelektrische Focussierung (IEF); Trennung von ungefaltetem und†gefaltetem Protein sowie von Faltungsisoformen; pH 3-10-¶Gradienten; Thiol-Affinitätschromatographie zur trägergebundenen©Renaturierung®™
85áRecombinant soluble human interleukin-6 receptor. Expression iníEscherichia coli, renaturation and purificationóúñ1993ÑPetersª13.06.1995º216¿239 245⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´Refolding; L-Arginin im Renaturierungspuffer (0.8 M); 0.1 M Tris-†HCl, pH 8.5; 10 mM/1 mM Glutathion (red/ox); 1 mM EDTA;¶Proteinkonzentration angeblich 100 mg/ml (!);©®™
86áSolublization and renaturation of overexpressed aggregates ofímutant tryptophan synthase a-subunitsóúñ1989ÑPetersª13.06.1995º55(5)¿1106 1111⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´Chaotrope Salze zur Solubilisierung (KSCN, NaI, NaNO3, LiBr,†CaCl2); Beste Ergebnisse mit KSCN (chaotropstes Salz lt.¶Hofmeister-Serie;©®™
87áStructural and functional roles of the cysteine residues in theía-subunit of the Escherichia coli tryptophan synthetase. I.óStructural roles and reactivity of the cysteine residuesúñ1969ÑPetersª13.06.1995º8¿2769 2781⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´Bestimmung der freien SH-Gruppen mit Ellmanns-Reagenz (DNTB);†¶©®™
88áIn vitro mutagenesis and overexpression of the Escherichia coliítrpA gene and the partial characterization of the resultantótryptophan synthase mutant a-subunitsúñ1986ÑPetersª13.06.1995º261(35)¿1660416615⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´30% Überexpression†¶©®™
89áTissue sulfhydryl groupsíóúñ1959ÑPetersª13.06.1995º82¿70 77⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´Methode zur Bestimmung freier SH-Gruppen (Cys) in Proteinen mit†DTNB (Ellman's Reagenz); Kalkulation freier SH-Gruppen; Genaue¶Vorschrift; Lineare Standardkurve©®™
90áSome species of human leukocyte interferon are glycosyltedíóúñ1984ÑPetersª13.06.1995º232(1)¿422 426⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´†¶©®™
91áA new and general procedure for refolding mutant Bowman-Birk-ítype proteinase inhibitors on trypsin-sepharose as a matrix withócomplementary structureúñ1989ÑPetersª13.06.1995º252(1,2)¿153 157⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´†¶©®™
92áIL-10 prevents naturally occuring fetal loss in the CBA x DBA/2ímating combination, and local defect in IL-10 production in thisóabortion-prone combination is corrected by in vivo injection ofúIFN-tñ1995ÑPetersª13.06.1995º154¿4261 4268⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´Ovines Interferon-Tau; oIFN-t†¶©®™
93áíóúñ1995ÑPetersª13.06.1995º¿⌐Biotransformations in organic chemistry - A textbook¬½¼Springer-Verlag¡Berlin, Heidelberg, New York«2»1 350ãõØøœŒÀÃÕ¨´†¶©®™
94áSynthesis and secretion of human epidermal growth factor byíEscherichia colióúñ1985ÑPetersª13.06.1995º82¿7212 7216⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´PHO-A-Signalsequenz-Konstrukt; Phosphat-Limitierung zur†Induktion des Stammes¶©®™
95áPurification of monoclonal antibodies from whole hybridomaífermentation broth by fluidized bed adsorptionóúñ1994ÑPetersª13.06.1995º45¿205 211⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´STREAMLINE-System; Hintergrunddaten†¶©®™
96áDas Interleukin-Netzwerkíóúñ1995ÑPetersª13.06.1995º2(1)¿8 13⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´Interleukin-4; Antagonisten; Mechanismen;†Hintergrundinformationen¶©®™
97áAntagonist design through forced electrostatic mismatchíóúñ1994ÑPetersª13.06.1995º1(10)¿674 676⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´†¶©®™
98áOn-line biomass monitoring by capacitance measurementíóúñ1992ÑPetersª13.06.1995º23¿303 314⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´†¶©®™
99áMethylotrophic yeast Pichia pastoris produced in high-cell-ídensity fermentations with high cell yields as vehicle forórecombinant protein productionúñ1989ÑPetersª13.06.1995º34¿403 404⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´Spurenelemente können limitierend bei der†Induktion/Produktbildung sein und die Ausbeute an heterologem¶Protein deutlich herabsetzen (15 auf 4 mg/l h); Medium;©®™
100áProduction and application of methylotrophic yeast Pichiaípastorisóúñ1988ÑPetersª13.06.1995º31¿44 49⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´Semikontinuierliche und kontinuierliche Fermentation steigert 10-†fach die Biomasse gegenüber batch-Fermentation¶©®™
101áHigh-productivity fermentation process for cultivatingíindustrial microorganismsóúñ1987ÑPetersª13.06.1995º2¿79 85⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´Zelldichten bis 120 g/l (CDW) erreichbar; definiertes Medium;†Ammonium als pH-Kontrolle und N-Quelle¶©®™
102áHigh-level expression of heterologous proteins in methylotrophicíyeast Pichia pastorisóúñ1988ÑPetersª13.06.1995º28¿265 278⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´Zelldichten bis 100 g/l Trockengewicht (CDW); Medium; definiert;†komplex;¶©®™
103áThe proton magentic-resonance spectra of cell-wall mannan fromíPichia pastoris and their changes depending on growth substrateóúñ1978ÑPetersª13.06.1995º42(4)¿897 898⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´†¶©®™
105áUnbekanntíóúñ1988ÑPetersª14.06.1995º7¿535 548⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´†¶©®™
106áType-I interferon inhibition of superantigen stimulation -íimplications for treatment of superantigen-associated diseaseóúñ1995ÑPetersª14.06.1995º15¿39 45⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´†¶©®™
107áFunctional properties of the recombinant kringle-2 domain ofítissue plasminogen activator produced in Escherichia colióúñ1990ÑPetersª14.06.1995º265(24)¿1460614611⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´†¶©®™
108áA novel method for the purification of porcine phospholipase A2íexpressed in E. colióúñ1991ÑPetersª14.06.1995º176(1)¿371 377⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´Chromatofocussierung; IEF; Renatureirung, Single-step†Aufreinigung; Sulfonierung; Renaturierung aus Harnstoff durch 1:¶5 Verdünnung; Glutathion-Redoxsystem (1:2 mM red:ox); Gua-©Solubilisierung, Sulfonierung, 1% Essigsäurefällung,®Resuspension in Harnstoff (5 M); Renaturierung (s.o.)™
109áExpression of porcine pancreatic phospholipase A2. Generation ofíactive enzyme by sequence-specific cleavage of a hybrid proteinófrom Escherichia coliúñ1987ÑPetersª14.06.1995º15(9)¿3743 3759⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´†¶©®™
111áMultiple forms of recombinant murine interleukin-4 expressed iníCOS-7 monkey kidney cellsóúñ1989ÑPetersª14.06.1995º1007¿283 288⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´CM-Sepharose, Sephadex G-100, Mono-S FPLC; 6 x 10^7 U/mg;†Glycosylierungsmuster; N-linked Saccharides¶©®™
112áDisulfide assignments in recombinant mouse and human interleukiní4óúñ1991ÑPetersª14.06.1995º30¿1515 1523⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´Unterschiede in Disulfidbrücken zwischen Maus- und human IL-4;†Nur eine von zwei N-Glykosylierungsstellen wird genutzt¶©®™
113áIsolation and characterization of multiple variants ofírecombinant human interleukin 4 expressed in mammalian cellsóúñ1988ÑPetersª14.06.1995º263(22)¿1081710823⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´†¶©®™
114áGlycosylation variants of murine interleukin-4: evidence forídifferent functional propertiesóúñ1992ÑPetersª14.06.1995º75¿143 149⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´Sezernierung von induzierten D10-Zellen; 3 unterschiedliche IL-4†Formen (SDS-PAGE, non-red.);¶©®™
115áPurification and characterization of recombinant humaníinterleukin 4óúñ1989ÑPetersª14.06.1995º262¿897 908⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´Saccharomyces cerevisiae; Fusionsprotein (C-terminal); pre-pro-a-†mating factor; (0.6-0.8 mg/l); ConA-Sepharose; S-Sepharose FF;¶C18-HPLC; Ausbeute 51% (0.3-0.4 mg/l);©®™
116áHuman trophoblast interferonsíóúñ1993ÑPetersª14.06.1995º22¿91 105⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´Cibacron-Blue-Affinitätschromatographie; Antigenic†characterization; chemical characterization; Antiviral¶activities; Inhibition of cell proliferation; Immunosuppressive©properties; Functions of IFN's in fetal and placental®protection; Regulation™
118áEffect of overproduction of heat shock chaperones GroESL andíDnaK on human procollagenase production in Escherichia colióúñ1992ÑPetersª14.06.1995º267(5)¿2849 2852⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´Both Chaperones caused a large increase in the apparent†solublity of a fusion of LamB signal peptide to procollagenase.¶GroESL had no effect on the accumulation of mature (secreted)©procoll., while DnaK suppressed secretion considerably. Absence®of signal pept. caused dramat. increase in solubility and accum.™
119áMechanisms and catalysts of disulfide bond formation in proteinsíóúñ1995ÑPetersª14.06.1995º13¿18 23⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´PDI: Protein disulfide isomerase; DsbA; DsbB; acidic pH: thiol-†exchange is slow; basic pH: thiol-exchange is fast; for BPTI the¶optimal Glutathion red:ox is 70:1©®™
120áSeparations in biotechnologyíóúñ1995ÑPetersª14.06.1995º13¿12 14⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´†¶©®™
121áThe oligosaccharides of glycoproteins: bioprocess factorsíaffecting oligosaccharide structure and their effect onóglycoprotein propertiesúñ1991ÑPetersª14.06.1995º9¿1347 1354⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´†¶©®™
122áProtein glycosylation in yeastíóúñ1987ÑPetersª14.06.1995º566¿915 944⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´†¶©®™
123áForeign gene expression in yeast: a reviewíóúñ1992ÑPetersª14.06.1995º8¿423 488⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´†¶©®™
124áHigh-level expression, purification, and characterization ofírecombinant human tumor necrosis factor synthesized in theómethylotrophic yeast Pichia pastorisúñ1989ÑPetersª14.06.1995º28¿4117 4125⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´†¶©®™
125áThe intracellular production and secretion of HIV-1 envelopeíprotein in the methylotrophic yeast Pichia pastorisóúñ1993ÑPetersª14.06.1995º136¿111 119⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´†¶©®™
126áFermentation development of recombionant Pichia pastorisíexpressing the heterologous gene: bovine lysozymeóúñ1990ÑPetersª14.06.1995º589¿350 362⌐¬½¼¡«»ãõØøœŒÀÃÕ¨´†¶©®™