메뉴 건너뛰기




Volumn 7, Issue 2, 1996, Pages 205-209

Role of physiology in the determination of protein heterogeneity

Author keywords

[No Author keywords available]

Indexed keywords

RECOMBINANT PROTEIN;

EID: 0029961609     PISSN: 09581669     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0958-1669(96)80014-0     Document Type: Article
Times cited : (6)

References (49)
  • 1
    • 0029294124 scopus 로고
    • Tissue-plasminogen activator coexpressed in Chinese-hamster ovary cells with a(2,6)-sialyltransferase contains NeuAc-α(2,6)Gal-β(1,4)GlcNAc linkages
    • Winch SL, Kallio PT, Bailey JE: Tissue-plasminogen activator coexpressed in Chinese-hamster ovary cells with a(2,6)-sialyltransferase contains NeuAc-α(2,6)Gal-β(1,4)GlcNAc linkages. Biotechnol Prog 1995, 11:348-351. See annotation for [2•].
    • (1995) Biotechnol Prog , vol.11 , pp. 348-351
    • Winch, S.L.1    Kallio, P.T.2    Bailey, J.E.3
  • 2
    • 0028979967 scopus 로고
    • Construction of stable BHK-21 cells coexpressing human secretory glycoproteins and human Gal(β-1-4)GlcNAc α-2,6-sialyltransferase. α-2,6-Linked NeuAc is preferentially attached to the Gal(β-1-4)GlcNAc(β-1-2)Man(α-1-3)-branch of diantennary oligosaccharides from secreted recombinant β-trace protein
    • Grabenhorst E, Hoffmann A, Nimtz M, Zettlmeissl G, Conradt HS: Construction of stable BHK-21 cells coexpressing human secretory glycoproteins and human Gal(β-1-4)GlcNAc α-2,6-sialyltransferase. α-2,6-Linked NeuAc is preferentially attached to the Gal(β-1-4)GlcNAc(β-1-2)Man(α-1-3)-branch of diantennary oligosaccharides from secreted recombinant β-trace protein. Eur J Biochem 1995, 232:718-725. This paper and [1•] demonstrate that genetic differences in the glycosylalion machinery between rodent and human cells can be minimized by expressing the appropriate glycosyltransferase.
    • (1995) Eur J Biochem , vol.232 , pp. 718-725
    • Grabenhorst, E.1    Hoffmann, A.2    Nimtz, M.3    Zettlmeissl, G.4    Conradt, H.S.5
  • 3
    • 0029065680 scopus 로고
    • N-glycosylation of recombinant human interferon-γ produced in different animal expression systems
    • James DC, Freedman RB, Hoare M, Ogonah OW, Rooney BC, Larionov OA, Dobrovolsky VN, Lagutin OV, Jenkins N: N-glycosylation of recombinant human interferon-γ produced in different animal expression systems. Biotechnology 1995, 13:592-596. A direct comparison of glycosylation of the same recombinant prolein expressed in three of the most popular eukaryotic expression systems.
    • (1995) Biotechnology , vol.13 , pp. 592-596
    • James, D.C.1    Freedman, R.B.2    Hoare, M.3    Ogonah, O.W.4    Rooney, B.C.5    Larionov, O.A.6    Dobrovolsky, V.N.7    Lagutin, O.V.8    Jenkins, N.9
  • 4
    • 0029636508 scopus 로고
    • Fluorophore labeled glycen analysis of immunoglobulin fusion proteins: Correlation of oligosaccharide content with in vivo clearance profile
    • Flesher AR, Marzowski J, Wang WC, Raff HV: Fluorophore labeled glycen analysis of immunoglobulin fusion proteins: correlation of oligosaccharide content with in vivo clearance profile. Biotechnol Bioeng 1995, 46:399-407. This paper highlights the importance of complex glycosylation in determining the clearance in vivo of recombinant glycoproteins. It ia the first comprehensive study of the relationship between recombinant protein glycosylation and half-life in vivo.
    • (1995) Biotechnol Bioeng , vol.46 , pp. 399-407
    • Flesher, A.R.1    Marzowski, J.2    Wang, W.C.3    Raff, H.V.4
  • 5
    • 0028765504 scopus 로고
    • Characterization of a recombinant antibody produced in the course of a high-yield fed-batch process
    • Robinson DK, Chan CP, Ip CY, Tsai PK, Tung J, Seamans TC, Lenny AB, Lee DK, Irwin J, Silberklang M: Characterization of a recombinant antibody produced in the course of a high-yield fed-batch process, Biotechnol Bioeng 1994, 44:727-735. A comprehensive study on the changes in recombinant protein N-glycosylation during the batch process. Results indicate the process is less efficient towards the end of culture.
    • (1994) Biotechnol Bioeng , vol.44 , pp. 727-735
    • Robinson, D.K.1    Chan, C.P.2    Ip, C.Y.3    Tsai, P.K.4    Tung, J.5    Seamans, T.C.6    Lenny, A.B.7    Lee, D.K.8    Irwin, J.9    Silberklang, M.10
  • 7
    • 0029014545 scopus 로고
    • Effect of different cell-culture conditions on the polypeptide integrity and N-glycosylation of a recombinant model glycoprotein
    • Gawlitzek M, Conradt HS, Wagner R: Effect of different cell-culture conditions on the polypeptide integrity and N-glycosylation of a recombinant model glycoprotein. Biotechnol Bioeng 1995, 46:536-544.
    • (1995) Biotechnol Bioeng , vol.46 , pp. 536-544
    • Gawlitzek, M.1    Conradt, H.S.2    Wagner, R.3
  • 8
    • 0029097924 scopus 로고
    • Characterization of changes in the glycosylation pattern of recombinant proteins from BHK-21 -cells due to different culture conditions
    • Gawlitzek M, Valley U, Nimtz M, Wagner R, Conradt HS: Characterization of changes in the glycosylation pattern of recombinant proteins from BHK-21 -cells due to different culture conditions. J Biotechnol 1995, 42:117-131.
    • (1995) J Biotechnol , vol.42 , pp. 117-131
    • Gawlitzek, M.1    Valley, U.2    Nimtz, M.3    Wagner, R.4    Conradt, H.S.5
  • 9
    • 0028909145 scopus 로고
    • The effect of increasing nucleotide sugar concentrations on the incorporation of sugars into glycoconjugates in rat hepatocytes
    • Rijcken WRP, Overdijk B, Vandeneijnden DH, Ferwerda W: The effect of increasing nucleotide sugar concentrations on the incorporation of sugars into glycoconjugates in rat hepatocytes. Biochem J 1995, 305:865-670,
    • (1995) Biochem J , vol.305 , pp. 865-1670
    • Rijcken, W.R.P.1    Overdijk, B.2    Vandeneijnden, D.H.3    Ferwerda, W.4
  • 10
    • 0028706975 scopus 로고
    • Effect of lipid supplements on the production and glycosylation of recombinant interferon-γ expressed in CHO cells
    • Jenkins N, Castro PML, Menon S, Ison AP, Bull AT: Effect of lipid supplements on the production and glycosylation of recombinant interferon-γ expressed in CHO cells. Cytotechnology 1994, 15:209-215.
    • (1994) Cytotechnology , vol.15 , pp. 209-215
    • Jenkins, N.1    Castro, P.M.L.2    Menon, S.3    Ison, A.P.4    Bull, A.T.5
  • 11
    • 0029053768 scopus 로고
    • Removal of sialic acid from a glycoprotein in CHO cell supernatant by action of an extracellular CHO cell slalidase
    • Gramer MJ, Goochee CF, Chock V, Brousseau DT, Sliwkowski MB: Removal of sialic acid from a glycoprotein in CHO cell supernatant by action of an extracellular CHO cell slalidase. Biotechnology 1995, 13:692-598. See annotation for [12*].
    • (1995) Biotechnology , vol.13 , pp. 692-1598
    • Gramer, M.J.1    Goochee, C.F.2    Chock, V.3    Brousseau, D.T.4    Sliwkowski, M.B.5
  • 12
    • 0028166666 scopus 로고
    • Glycosidase activities of the 293 and NSO cell-lines, and of an antibody-producing hybridoma cell-line
    • Gramer MJ, Goochee CF: Glycosidase activities of the 293 and NSO cell-lines, and of an antibody-producing hybridoma cell-line. Biotechnol Bioeng 1994, 43:423-428. This paper and [11*] compare the exoglycosidase activities found in the supernatant of mammalian host cell lines used for recombinant protein production.
    • (1994) Biotechnol Bioeng , vol.43 , pp. 423-428
    • Gramer, M.J.1    Goochee, C.F.2
  • 15
    • 0028349781 scopus 로고
    • Site specific characterization of glycoprotein carbohydrates by exoglycosidase digestion and laser desorptlon mass spectrometry
    • Sutton CW, O'Neill JA, Cottrell JS: Site specific characterization of glycoprotein carbohydrates by exoglycosidase digestion and laser desorptlon mass spectrometry. Anal Biochem 1904, 218:34-46.
    • (1904) Anal Biochem , vol.218 , pp. 34-46
    • Sutton, C.W.1    O'Neill, J.A.2    Cottrell, J.S.3
  • 18
    • 0028962142 scopus 로고
    • Site-specific detection and structural characterization of the glycosylation of human plasma-proteins lecithin-cholesterol acyltransferase and apolipoprotein-D using HPLC/electrospray mass-spectrometry and sequential glycosidase digestion
    • Schindler PA, Settineri CA, Collet X, Fielding CJ, Burlingame AL: Site-specific detection and structural characterization of the glycosylation of human plasma-proteins lecithin-cholesterol acyltransferase and apolipoprotein-D using HPLC/electrospray mass-spectrometry and sequential glycosidase digestion. Protein Sci 1995, 4:791-803.
    • (1995) Protein Sci , vol.4 , pp. 791-803
    • Schindler, P.A.1    Settineri, C.A.2    Collet, X.3    Fielding, C.J.4    Burlingame, A.L.5
  • 19
    • 0028957067 scopus 로고
    • Structural-analysis of the sialylated N-linked and O-linked carbohydrate chains of recombinant-humen-erythropoietin expressed in Chinese hamster ovary cells - Sialylation patterns and branch location of dimeric N-acetyliactosamine units
    • Hokke CH, Bergwerff AA, Vandederr, GWK, Kamerling JP, Vliegenthart JFG: Structural-analysis of the sialylated N-linked and O-linked carbohydrate chains of recombinant-humen-erythropoietin expressed in Chinese hamster ovary cells - sialylation patterns and branch location of dimeric N-acetyliactosamine units. Eur J Biochem 1995, 228:981-1008.
    • (1995) Eur J Biochem , vol.228 , pp. 981-1008
    • Hokke, C.H.1    Bergwerff, A.A.2    Vandederr, G.W.K.3    Kamerling, J.P.4    Vliegenthart, J.F.G.5
  • 20
    • 0028952933 scopus 로고
    • Characterization of the glycosylation of a human-IgM produced by a human-mouse hybridoma
    • Monica TJ, Williams SB, Goochee CF, Maiorella BL: Characterization of the glycosylation of a human-IgM produced by a human-mouse hybridoma. Glycobiology 1995, 5:175-185. This paper reveals the glycosylation profile of recombinant IgM to be substantially different from that of IgG. Most notably, the ion-exchange technique demonstrates more complex glycan structures on IgM compared with IgG; this may reflect steric hindrance around the IgG Fc glycosylation site.
    • (1995) Glycobiology , vol.5 , pp. 175-185
    • Monica, T.J.1    Williams, S.B.2    Goochee, C.F.3    Maiorella, B.L.4
  • 21
    • 0027957068 scopus 로고
    • Monosaccharide and oligosaccharide analysis of isoelectric focusing-separated and blotted granulocyte-colony-stimulating factor glycoforms using high-pH anion-exchange chromatography with pulsed amperometric detection
    • Andersen DC, Goochee CF, Cooper G, Weitzhandler M: Monosaccharide and oligosaccharide analysis of isoelectric focusing-separated and blotted granulocyte-colony-stimulating factor glycoforms using high-pH anion-exchange chromatography with pulsed amperometric detection. Glycobiology 1994, 4:459-467-
    • (1994) Glycobiology , vol.4
    • Andersen, D.C.1    Goochee, C.F.2    Cooper, G.3    Weitzhandler, M.4
  • 22
    • 0028280439 scopus 로고
    • Structural-analysis of the N-glycans from human-immunoglobulin A1 - Comparison of normal human serum immunoglobulin A1 with that isolated from patients with rheumatoid-arthritis
    • Field MC, Amatayakulchantler S, Rademacher TW, Rudd PM, Dwek RA: Structural-analysis of the N-glycans from human-immunoglobulin A1 - comparison of normal human serum immunoglobulin A1 with that isolated from patients with rheumatoid-arthritis. Biochem J 1994, 299:261-275.
    • (1994) Biochem J , vol.299 , pp. 261-275
    • Field, M.C.1    Amatayakulchantler, S.2    Rademacher, T.W.3    Rudd, P.M.4    Dwek, R.A.5
  • 23
    • 0029144642 scopus 로고
    • Multiple sequential fraction collection of peptides and glycopeptides by high-performance capillary electrophoresis
    • Boss HJ, Rohde MF, Rush RS: Multiple sequential fraction collection of peptides and glycopeptides by high-performance capillary electrophoresis. Anal Biochem 1995, 230:123-129.
    • (1995) Anal Biochem , vol.230 , pp. 123-129
    • Boss, H.J.1    Rohde, M.F.2    Rush, R.S.3
  • 24
    • 0028173035 scopus 로고
    • High resolution separation of recombinant human interferon-γ by micellar electrokinetic capillary chromatography
    • James DC, Freedman RB, Hoare M, Jerkins N: High resolution separation of recombinant human interferon-γ by micellar electrokinetic capillary chromatography. Anal Biochem 1094, 222:315-322.
    • (1094) Anal Biochem , vol.222 , pp. 315-322
    • James, D.C.1    Freedman, R.B.2    Hoare, M.3    Jerkins, N.4
  • 25
    • 0029083855 scopus 로고
    • High-resolution and rapid analysis of branched oligosaccharides by capiliary electrophoresis
    • Camilleri P, Harland GB, Okafo G: High-resolution and rapid analysis of branched oligosaccharides by capiliary electrophoresis. Anal Biochem 1995, 230:115-122. Describes the use of a CE system for the rapid fingerprinting of glycan structures on glycoproteins.
    • (1995) Anal Biochem , vol.230 , pp. 115-122
    • Camilleri, P.1    Harland, G.B.2    Okafo, G.3
  • 26
    • 0001944475 scopus 로고
    • Characterization of 9-aminopyrene-1,4,6-trisulfonate-derivatized sugars by capillary electrophoresis with laser-induced fluorescence detection
    • Evangelista RA, Liu MS, Chen FTA: Characterization of 9-aminopyrene-1,4,6-trisulfonate-derivatized sugars by capillary electrophoresis with laser-induced fluorescence detection, Anal Chem 1995, 67:2239-2245.
    • (1995) Anal Chem , vol.67 , pp. 2239-2245
    • Evangelista, R.A.1    Liu, M.S.2    Chen, F.T.A.3
  • 27
    • 0028022532 scopus 로고
    • Quantitative-determination of monosaccharides in glycoproteins by high-performance liquid-chromatography with highly sensitive fluorescence detection
    • Anumula KR: Quantitative-determination of monosaccharides in glycoproteins by high-performance liquid-chromatography with highly sensitive fluorescence detection. Anal Biochem 1994, 230:275-283.
    • (1994) Anal Biochem , vol.230 , pp. 275-283
    • Anumula, K.R.1
  • 28
    • 0029115046 scopus 로고
    • Rapid quantitative-determination of sialic acids in glycoproteins by high-performance liquid-chromatography with a sensitive fluorescence detection
    • Anumula KR: Rapid quantitative-determination of sialic acids in glycoproteins by high-performance liquid-chromatography with a sensitive fluorescence detection. Anal Biochem 1995, 230:24-30.
    • (1995) Anal Biochem , vol.230 , pp. 24-30
    • Anumula, K.R.1
  • 29
    • 0029164230 scopus 로고
    • Nonselective and efficient fluorescent labeling of glycans using 2-amino benzamide and anthranilic acid
    • Bigge JC, Patel TP, Bruce JA, Goulding PN, Charles SM, Parekh RB: Nonselective and efficient fluorescent labeling of glycans using 2-amino benzamide and anthranilic acid. Anal Biochem 1995, 230:229-238, Reports a versatile label, 2-amino benzamide, that is compatible with many types of subsequent glycosylalion analysis,
    • (1995) Anal Biochem , vol.230 , pp. 229-238
    • Bigge, J.C.1    Patel, T.P.2    Bruce, J.A.3    Goulding, P.N.4    Charles, S.M.5    Parekh, R.B.6
  • 30
    • 0029011531 scopus 로고
    • Isoelectric-focusing as a tool for the investigation of post-translational processing and chemical modifications of proteins
    • Gianazza E: Isoelectric-focusing as a tool for the investigation of post-translational processing and chemical modifications of proteins. J Chromatography A 1995, 705:67-87.
    • (1995) J Chromatography A , vol.705 , pp. 67-87
    • Gianazza, E.1
  • 31
    • 0029035876 scopus 로고
    • Endoproteolytic processing of recombinant proalbumin variants by the yeast Kex2 protease
    • Ledgerwood EC, George PM, Peach RJ, Brennan SO: Endoproteolytic processing of recombinant proalbumin variants by the yeast Kex2 protease. Biochem J 1995, 308:321-325.
    • (1995) Biochem J , vol.308 , pp. 321-325
    • Ledgerwood, E.C.1    George, P.M.2    Peach, R.J.3    Brennan, S.O.4
  • 32
    • 0029115204 scopus 로고
    • Production of recombinant bovine enterokinase catalytic subunit in Escherichia cell using the novel secretory fusion partner DsbA
    • Collinsracie LA, McColgan JM, Grant KL, Diblasiosmith EA, MrCoy JM, Lavallie ER: Production of recombinant bovine enterokinase catalytic subunit in Escherichia cell using the novel secretory fusion partner DsbA. Biotechnology 1995, 13:982-987. Presents a novel technique for ensuring correct proteolytic processing of a human protein in prokaryotic host cells. In this approach, the required protease is co-expressed in-frame with the fusion protein of choice
    • (1995) Biotechnology , vol.13 , pp. 982-987
    • Collinsracie, L.A.1    McColgan, J.M.2    Grant, K.L.3    Diblasiosmith, E.A.4    Mrcoy, J.M.5    Lavallie, E.R.6
  • 33
    • 0028674222 scopus 로고
    • Purification of recombinant soluble forms of furin produced in Chinese hamster ovary cells
    • Nakayama K: Purification of recombinant soluble forms of furin produced in Chinese hamster ovary cells. Methods Enzymol 1994, 244:167-175.
    • (1994) Methods Enzymol , vol.244 , pp. 167-175
    • Nakayama, K.1
  • 34
    • 0028861480 scopus 로고
    • Endoproteolytic cleavage of its propeptide is a prerequisite for efficient transport of furin out of the endoplasmic-reticulum
    • Creamers JWM, Vey M. Schafer W, Ayoubi TAY, Roebroek AJM, Klenk HD, Garten W, Vandeven WJM: Endoproteolytic cleavage of its propeptide is a prerequisite for efficient transport of furin out of the endoplasmic-reticulum. J Biol Chem 1995, 270:2695-2702. See annotation for [35•].
    • (1995) J Biol Chem , vol.270 , pp. 2695-2702
    • Creamers, J.W.M.1    Vey, M.2    Schafer, W.3    Ayoubi, T.A.Y.4    Roebroek, A.J.M.5    Klenk, H.D.6    Garten, W.7    Vandeven, W.J.M.8
  • 35
    • 0028605962 scopus 로고
    • Maturation of the trans-Golgi network protease furin - Compartmentalization of propeptide removal, substrate cleavage, and COOH-terminal truncation
    • Vey M, Schafer W, Berghofer S, Klenk HD, Garten W: Maturation of the trans-Golgi network protease furin - compartmentalization of propeptide removal, substrate cleavage, and COOH-terminal truncation. J Cell Biol 1994, 127:1829-1842. This cytology study and [34•] provide important information on the maturation and cleavage of the mammalian endoprotease furin. The authors trace the localization of pro-furin and the mature protease.
    • (1994) J Cell Biol , vol.127 , pp. 1829-1842
    • Vey, M.1    Schafer, W.2    Berghofer, S.3    Klenk, H.D.4    Garten, W.5
  • 36
    • 0029020219 scopus 로고
    • Direct role of furin in mammalian prosomatostatin processing
    • Galanopoulou AS, Seidah NG, Patel YC: Direct role of furin in mammalian prosomatostatin processing. Biochem J 1995, 309:33-40.
    • (1995) Biochem J , vol.309 , pp. 33-40
    • Galanopoulou, A.S.1    Seidah, N.G.2    Patel, Y.C.3
  • 37
    • 0028960688 scopus 로고
    • Engineered serine-protease inhibitor prevents furin-catalyzed activation of the fusion glycoprotein and production of infectious measles virus
    • Watanabe M, Hirano A, Stenglein S, Nelson J, Thomas G, Wong TC: Engineered serine-protease inhibitor prevents furin-catalyzed activation of the fusion glycoprotein and production of infectious measles virus. J Virol 1995, 69:3206-3210. See annotation for [38•].
    • (1995) J Virol , vol.69 , pp. 3206-3210
    • Watanabe, M.1    Hirano, A.2    Stenglein, S.3    Nelson, J.4    Thomas, G.5    Wong, T.C.6
  • 38
    • 0028116527 scopus 로고
    • Heterologous expression of the human D2S dopamine-receptor in protease-deficient Saccharomyces cerevisiae strains
    • Sander P, Grunewald S, Bach M, Haase W, Reilander H, Michel H: Heterologous expression of the human D2S dopamine-receptor in protease-deficient Saccharomyces cerevisiae strains. Eur J Biochem 1994, 226:697-705. This paper and [37•] suggest strategies for minimizing proteolytic degradation of recombinant proteins; mutant host lines are selected with minimal endogenous protease activity.
    • (1994) Eur J Biochem , vol.226 , pp. 697-705
    • Sander, P.1    Grunewald, S.2    Bach, M.3    Haase, W.4    Reilander, H.5    Michel, H.6
  • 39
    • 0028878753 scopus 로고
    • Detection of synthetic protein isomers and conformers by electrospray mass-spectrometry
    • Muir TW, Williams MJ, Kent SBH: Detection of synthetic protein isomers and conformers by electrospray mass-spectrometry. Anal Biochem 1995, 224:100-109.
    • (1995) Anal Biochem , vol.224 , pp. 100-109
    • Muir, T.W.1    Williams, M.J.2    Kent, S.B.H.3
  • 40
    • 0000745288 scopus 로고
    • Characterization of disulfide linkages and disulfide bond scrambling in recombinant human macrophage-colony-stimulating factor by fast-atom bombardment mass-spectrometry of enzymatic digests
    • Glocker MO, Arbogast B, Deinzer ML: Characterization of disulfide linkages and disulfide bond scrambling in recombinant human macrophage-colony-stimulating factor by fast-atom bombardment mass-spectrometry of enzymatic digests. J Am Soc Mass Spectrom 1995, 6:638-643. These authors describe an important analytical technique for the characterization of disulphide bond formation. The mass spectra of untreated peptides and of peptides subjected to limited proteolysis are compared. Proteolysis preserves disulphide bonding and can be used to assign specific cysteine pairings.
    • (1995) J am Soc Mass Spectrom , vol.6 , pp. 638-643
    • Glocker, M.O.1    Arbogast, B.2    Deinzer, M.L.3
  • 41
    • 0028946717 scopus 로고
    • Intracellular folding of tissue-type plasminogen-activator - Effects of disulfide bond formation on N-linked glycosylation and secretion
    • Allen S, Naim HY, Bulleid NJ: Intracellular folding of tissue-type plasminogen-activator - effects of disulfide bond formation on N-linked glycosylation and secretion. J Biol Chem 1995, 270:4797-4804.
    • (1995) J Biol Chem , vol.270 , pp. 4797-4804
    • Allen, S.1    Naim, H.Y.2    Bulleid, N.J.3
  • 42
    • 0027996296 scopus 로고
    • Deamidation of asparagine and glutamine residues in proteins and peptides - Structural determinants and analytical methodology
    • Bischoff R, Kolbe HVJ: Deamidation of asparagine and glutamine residues in proteins and peptides - structural determinants and analytical methodology. J Chromatogr B 1994, 662:261-278. A useful review of methods and causes of deamidation.
    • (1994) J Chromatogr B , vol.662 , pp. 261-278
    • Bischoff, R.1    Kolbe, H.V.J.2
  • 43
    • 0029075220 scopus 로고
    • Effect of adjacent histidine and cysteine residues on the spontaneous degradation of asparaginyl-containing and aspartyl-containing peptides
    • Brenn an TV, Clarke S: Effect of adjacent histidine and cysteine residues on the spontaneous degradation of asparaginyl-containing and aspartyl-containing peptides. Int J Pept Protein Res 1995, 45:547-553.
    • (1995) Int J Pept Protein Res , vol.45 , pp. 547-553
    • Brenn An, T.V.1    Clarke, S.2
  • 44
    • 0028931574 scopus 로고
    • Evidence for a common intermediate in insulin deamidation and covalent dimer formation-effects of pH and aniline trapping in dilute acidic solutions
    • Darrington RT, Anderson BD: Evidence for a common intermediate in insulin deamidation and covalent dimer formation-effects of pH and aniline trapping in dilute acidic solutions. J Pharm Sci 1995, 84:275-262.
    • (1995) J Pharm Sci , vol.84 , pp. 275-1262
    • Darrington, R.T.1    Anderson, B.D.2
  • 45
    • 0029240481 scopus 로고
    • Expression and purification of a human recombinant methyltransferase that repairs damaged proteins
    • MacLaren DC, Clarke S: Expression and purification of a human recombinant methyltransferase that repairs damaged proteins. Protein Exp Puril 1995, 6:99-108. Describes the production and purification of recombinant methyltransferase, a useful enzyme for the repair of damaged L-aspartyl residues. This is the first study where expression of a recombinant enzyme has been used to repair a damaged protein in vivo.
    • (1995) Protein Exp Puril , vol.6 , pp. 99-108
    • MacLaren, D.C.1    Clarke, S.2
  • 46
    • 0029048654 scopus 로고
    • Characterization of tyrocidine synthetase-1 (TY1)-requirement of post-translational modification for peptide biosynthesis
    • Pfeifer E, Pavelavrancic M, Vondohren H, Kleinkauf H: Characterization of tyrocidine synthetase-1 (TY1)-requirement of post-translational modification for peptide biosynthesis. Biochemistry 1995, 34:7450-7459.
    • (1995) Biochemistry , vol.34 , pp. 7450-7459
    • Pfeifer, E.1    Pavelavrancic, M.2    Vondohren, H.3    Kleinkauf, H.4
  • 48
    • 0028900550 scopus 로고
    • Involvement of N-myristoylation in monoclonal-antibody recognition sites on chimeric G-protein α-subunits
    • Justice JM, Bliziotes MM, Stevens LA, Moss J, Vaughan M: Involvement of N-myristoylation in monoclonal-antibody recognition sites on chimeric G-protein α-subunits. J Biol Chem 1995, 270:6436-6439.
    • (1995) J Biol Chem , vol.270 , pp. 6436-6439
    • Justice, J.M.1    Bliziotes, M.M.2    Stevens, L.A.3    Moss, J.4    Vaughan, M.5
  • 49
    • 0028918064 scopus 로고
    • Phosphoric-acid entrapment leads to apparent protein heterogeneity
    • Fountoulakis M, Vilbois F, Oesterhelt G, Vetter W: Phosphoric-acid entrapment leads to apparent protein heterogeneity. Biotechnology 1995, 13:383-388. A salutary lesson for those involved in the analysis of protein heterogeneity. Extra bands observed in gel electrophoresis are found to be due to the entrapment of phosphoric acid.
    • (1995) Biotechnology , vol.13 , pp. 383-388
    • Fountoulakis, M.1    Vilbois, F.2    Oesterhelt, G.3    Vetter, W.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.