Characterization of recombinant human interleukin-2 with micromethods
Highly purified recombinant human interleukin-2, expressed in Escherichia coli, was analyzed by micromethods. N-Terminal sequence analysis showed that methionine at position 0 was found in 90% of the molecules and not completely removed in post-ribosomal processing. A complete peptide map of the red...
Ausführliche Beschreibung
Gespeichert in:
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
1985 |
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| Reproduktion: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
|---|---|
| Übergeordnetes Werk: |
in: Journal of Chromatography A - Amsterdam : Elsevier, 326(1985), Seite 357-361 |
| Übergeordnetes Werk: |
volume:326 ; year:1985 ; pages:357-361 |
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NLEJ174137419 |
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| 520 | |a Highly purified recombinant human interleukin-2, expressed in Escherichia coli, was analyzed by micromethods. N-Terminal sequence analysis showed that methionine at position 0 was found in 90% of the molecules and not completely removed in post-ribosomal processing. A complete peptide map of the reduced and S-carboxymethylated protein was obtained by high-performance liquid chromatography after tryptic digestion, and the fragments were identified by amino acid analysis and automated Edman sequence analysis. Using a double-label S-carboxymethylation procedure, it was determined that there is a disulfide linkage between the cysteine residues at positions 58 and 105. The third cysteine residue at position 125 was found to be present as the free sulfhydryl. | ||
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(DE-627)NLEJ174137419 (DE-599)GBVNLZ174137419 DE-627 ger DE-627 rakwb eng Characterization of recombinant human interleukin-2 with micromethods 1985 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Highly purified recombinant human interleukin-2, expressed in Escherichia coli, was analyzed by micromethods. N-Terminal sequence analysis showed that methionine at position 0 was found in 90% of the molecules and not completely removed in post-ribosomal processing. A complete peptide map of the reduced and S-carboxymethylated protein was obtained by high-performance liquid chromatography after tryptic digestion, and the fragments were identified by amino acid analysis and automated Edman sequence analysis. Using a double-label S-carboxymethylation procedure, it was determined that there is a disulfide linkage between the cysteine residues at positions 58 and 105. The third cysteine residue at position 125 was found to be present as the free sulfhydryl. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Lahm, H.-W. oth Stein, S. oth in Journal of Chromatography A Amsterdam : Elsevier 326(1985), Seite 357-361 (DE-627)NLEJ17403282X (DE-600)1491247-8 0021-9673 nnns volume:326 year:1985 pages:357-361 http://linkinghub.elsevier.com/retrieve/pii/S0021-9673(01)87461-6 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 326 1985 357-361 |
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(DE-627)NLEJ174137419 (DE-599)GBVNLZ174137419 DE-627 ger DE-627 rakwb eng Characterization of recombinant human interleukin-2 with micromethods 1985 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Highly purified recombinant human interleukin-2, expressed in Escherichia coli, was analyzed by micromethods. N-Terminal sequence analysis showed that methionine at position 0 was found in 90% of the molecules and not completely removed in post-ribosomal processing. A complete peptide map of the reduced and S-carboxymethylated protein was obtained by high-performance liquid chromatography after tryptic digestion, and the fragments were identified by amino acid analysis and automated Edman sequence analysis. Using a double-label S-carboxymethylation procedure, it was determined that there is a disulfide linkage between the cysteine residues at positions 58 and 105. The third cysteine residue at position 125 was found to be present as the free sulfhydryl. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Lahm, H.-W. oth Stein, S. oth in Journal of Chromatography A Amsterdam : Elsevier 326(1985), Seite 357-361 (DE-627)NLEJ17403282X (DE-600)1491247-8 0021-9673 nnns volume:326 year:1985 pages:357-361 http://linkinghub.elsevier.com/retrieve/pii/S0021-9673(01)87461-6 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 326 1985 357-361 |
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(DE-627)NLEJ174137419 (DE-599)GBVNLZ174137419 DE-627 ger DE-627 rakwb eng Characterization of recombinant human interleukin-2 with micromethods 1985 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Highly purified recombinant human interleukin-2, expressed in Escherichia coli, was analyzed by micromethods. N-Terminal sequence analysis showed that methionine at position 0 was found in 90% of the molecules and not completely removed in post-ribosomal processing. A complete peptide map of the reduced and S-carboxymethylated protein was obtained by high-performance liquid chromatography after tryptic digestion, and the fragments were identified by amino acid analysis and automated Edman sequence analysis. Using a double-label S-carboxymethylation procedure, it was determined that there is a disulfide linkage between the cysteine residues at positions 58 and 105. The third cysteine residue at position 125 was found to be present as the free sulfhydryl. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Lahm, H.-W. oth Stein, S. oth in Journal of Chromatography A Amsterdam : Elsevier 326(1985), Seite 357-361 (DE-627)NLEJ17403282X (DE-600)1491247-8 0021-9673 nnns volume:326 year:1985 pages:357-361 http://linkinghub.elsevier.com/retrieve/pii/S0021-9673(01)87461-6 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 326 1985 357-361 |
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(DE-627)NLEJ174137419 (DE-599)GBVNLZ174137419 DE-627 ger DE-627 rakwb eng Characterization of recombinant human interleukin-2 with micromethods 1985 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Highly purified recombinant human interleukin-2, expressed in Escherichia coli, was analyzed by micromethods. N-Terminal sequence analysis showed that methionine at position 0 was found in 90% of the molecules and not completely removed in post-ribosomal processing. A complete peptide map of the reduced and S-carboxymethylated protein was obtained by high-performance liquid chromatography after tryptic digestion, and the fragments were identified by amino acid analysis and automated Edman sequence analysis. Using a double-label S-carboxymethylation procedure, it was determined that there is a disulfide linkage between the cysteine residues at positions 58 and 105. The third cysteine residue at position 125 was found to be present as the free sulfhydryl. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Lahm, H.-W. oth Stein, S. oth in Journal of Chromatography A Amsterdam : Elsevier 326(1985), Seite 357-361 (DE-627)NLEJ17403282X (DE-600)1491247-8 0021-9673 nnns volume:326 year:1985 pages:357-361 http://linkinghub.elsevier.com/retrieve/pii/S0021-9673(01)87461-6 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 326 1985 357-361 |
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(DE-627)NLEJ174137419 (DE-599)GBVNLZ174137419 DE-627 ger DE-627 rakwb eng Characterization of recombinant human interleukin-2 with micromethods 1985 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Highly purified recombinant human interleukin-2, expressed in Escherichia coli, was analyzed by micromethods. N-Terminal sequence analysis showed that methionine at position 0 was found in 90% of the molecules and not completely removed in post-ribosomal processing. A complete peptide map of the reduced and S-carboxymethylated protein was obtained by high-performance liquid chromatography after tryptic digestion, and the fragments were identified by amino acid analysis and automated Edman sequence analysis. Using a double-label S-carboxymethylation procedure, it was determined that there is a disulfide linkage between the cysteine residues at positions 58 and 105. The third cysteine residue at position 125 was found to be present as the free sulfhydryl. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Lahm, H.-W. oth Stein, S. oth in Journal of Chromatography A Amsterdam : Elsevier 326(1985), Seite 357-361 (DE-627)NLEJ17403282X (DE-600)1491247-8 0021-9673 nnns volume:326 year:1985 pages:357-361 http://linkinghub.elsevier.com/retrieve/pii/S0021-9673(01)87461-6 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 326 1985 357-361 |
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Highly purified recombinant human interleukin-2, expressed in Escherichia coli, was analyzed by micromethods. N-Terminal sequence analysis showed that methionine at position 0 was found in 90% of the molecules and not completely removed in post-ribosomal processing. A complete peptide map of the reduced and S-carboxymethylated protein was obtained by high-performance liquid chromatography after tryptic digestion, and the fragments were identified by amino acid analysis and automated Edman sequence analysis. Using a double-label S-carboxymethylation procedure, it was determined that there is a disulfide linkage between the cysteine residues at positions 58 and 105. The third cysteine residue at position 125 was found to be present as the free sulfhydryl. |
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Highly purified recombinant human interleukin-2, expressed in Escherichia coli, was analyzed by micromethods. N-Terminal sequence analysis showed that methionine at position 0 was found in 90% of the molecules and not completely removed in post-ribosomal processing. A complete peptide map of the reduced and S-carboxymethylated protein was obtained by high-performance liquid chromatography after tryptic digestion, and the fragments were identified by amino acid analysis and automated Edman sequence analysis. Using a double-label S-carboxymethylation procedure, it was determined that there is a disulfide linkage between the cysteine residues at positions 58 and 105. The third cysteine residue at position 125 was found to be present as the free sulfhydryl. |
| abstract_unstemmed |
Highly purified recombinant human interleukin-2, expressed in Escherichia coli, was analyzed by micromethods. N-Terminal sequence analysis showed that methionine at position 0 was found in 90% of the molecules and not completely removed in post-ribosomal processing. A complete peptide map of the reduced and S-carboxymethylated protein was obtained by high-performance liquid chromatography after tryptic digestion, and the fragments were identified by amino acid analysis and automated Edman sequence analysis. Using a double-label S-carboxymethylation procedure, it was determined that there is a disulfide linkage between the cysteine residues at positions 58 and 105. The third cysteine residue at position 125 was found to be present as the free sulfhydryl. |
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